DB code: M00151
| CATH domain | 1.10.620.20 : Ribonucleotide Reductase, subunit A | Catalytic domain |
|---|---|---|
| 1.10.620.20 : Ribonucleotide Reductase, subunit A | ||
| 1.20.1280.10 : Monooxygenase | ||
| 1.20.1280.30 : Monooxygenase | ||
| E.C. | 1.14.13.25 | |
| CSA | 1mhy | |
| M-CSA | 1mhy | |
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 1.10.620.20 : Ribonucleotide Reductase, subunit A | S00028 M00204 M00205 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| P22869 |
Methane monooxygenase component A alpha chain
|
EC
1.14.13.25
Methane hydroxylase |
YP_113659.1
(Protein)
NC_002977.6 (DNA/RNA sequence) |
PF02332
(Phenol_Hydrox)
[Graphical View] |
| P27353 |
Methane monooxygenase component A alpha chain
|
EC
1.14.13.25
Methane hydroxylase |
PF02332
(Phenol_Hydrox)
[Graphical View] |
|
| P18798 |
Methane monooxygenase component A beta chain
|
EC
1.14.13.25
Methane hydroxylase |
YP_113660.1
(Protein)
NC_002977.6 (DNA/RNA sequence) |
PF02332
(Phenol_Hydrox)
[Graphical View] |
| P27354 |
Methane monooxygenase component A beta chain
|
EC
1.14.13.25
Methane hydroxylase |
PF02332
(Phenol_Hydrox)
[Graphical View] |
|
| P11987 |
Methane monooxygenase component A gamma chain
|
EC
1.14.13.25
Methane hydroxylase |
YP_113663.1
(Protein)
NC_002977.6 (DNA/RNA sequence) |
PF02964
(MeMO_Hyd_G)
[Graphical View] |
| P27355 |
Methane monooxygenase component A gamma chain
|
EC
1.14.13.25
Methane hydroxylase |
PF02964
(MeMO_Hyd_G)
[Graphical View] |
| KEGG enzyme name |
|---|
|
methane monooxygenase
methane hydroxylase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P22869 | MEMA_METCA | Methane + NAD(P)H + O(2) = methanol + NAD(P)(+) + H(2)O. | M.capsulatus has two forms of methane monooxygenase, a soluble and a membrane-bound type. The soluble type consists of four components (A to D): protein A, comprising three chains, in an alpha-2, beta-2, gamma-2 configuration, is a nonheme iron protein containing an unusual mu-hydroxo bridge structure at its active site and interacts with both oxygen and methane. | Binds 2 iron ions. | |
| P27353 | MEMA_METTR | Methane + NAD(P)H + O(2) = methanol + NAD(P)(+) + H(2)O. | M.trichosporium has two forms of methane monooxygenase, a soluble and a membrane-bound type. The soluble type consists of four components (A to D): protein A, comprising three chains, in an alpha-2, beta-2, gamma-2 configuration, is a nonheme iron protein containing an unusual mu-hydroxo bridge structure at its active site and interacts with both oxygen and methane. | Binds 2 iron ions. | |
| P18798 | MEMB_METCA | Methane + NAD(P)H + O(2) = methanol + NAD(P)(+) + H(2)O. | M.capsulatus has two forms of methane monooxygenase, a soluble and a membrane-bound type. The soluble type consists of four components (A to D): protein A, comprising three chains, in an alpha-2, beta-2, gamma-2 configuration, is a nonheme iron protein containing an unusual mu-hydroxo bridge structure at its active site and interacts with both oxygen and methane. | ||
| P27354 | MEMB_METTR | Methane + NAD(P)H + O(2) = methanol + NAD(P)(+) + H(2)O. | M.trichosporium has two forms of methane monooxygenase, a soluble and a membrane-bound type. The soluble type consists of four components (A to D): protein A, comprising three chains, in an alpha-2, beta-2, gamma-2 configuration, is a nonheme iron protein containing an unusual mu-hydroxo bridge structure at its active site and interacts with both oxygen and methane. | ||
| P11987 | MEMG_METCA | Methane + NAD(P)H + O(2) = methanol + NAD(P)(+) + H(2)O. | M.capsulatus has two forms of methane monooxygenase, a soluble and a membrane-bound type. The soluble type consists of four components (A to D): protein A, comprising three chains, in an alpha-2, beta-2, gamma-2 configuration, is a nonheme iron protein containing an unusual mu-hydroxo bridge structure at its active site and interacts with both oxygen and methane. | ||
| P27355 | MEMG_METTR | Methane + NAD(P)H + O(2) = methanol + NAD(P)(+) + H(2)O. | M.trichosporium has two forms of methane monooxygenase, a soluble and a membrane-bound type. The soluble type consists of four components (A to D): protein A, comprising three chains, in an alpha-2, beta-2, gamma-2 configuration, is a nonheme iron protein containing an unusual mu-hydroxo bridge structure at its active site and interacts with both oxygen and methane. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00680 | Methane metabolism |
| Compound table | ||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | |||||||||||||
| KEGG-id | C00023 | C01438 | C00007 | C00080 | C00005 | C00004 | C00132 | C00001 | C00006 | C00003 | ||||||
| E.C. | ||||||||||||||||
| Compound | Iron | Methane | O2 | H+ | NADPH | NADH | Methanol | H2O | NADP+ | NAD+ | ||||||
| Type | heavy metal | others | others | others | amide group,amine group,nucleotide | amide group,amine group,nucleotide | carbohydrate | H2O | amide group,amine group,nucleotide | amide group,amine group,nucleotide | ||||||
| ChEBI |
18248 82664 18248 82664 |
16183 16183 |
15379 26689 27140 15379 26689 27140 |
15378 15378 |
16474 16474 |
16908 16908 |
17790 17790 |
15377 15377 |
18009 18009 |
15846 15846 |
||||||
| PubChem |
23925 23925 |
297 297 |
977 977 |
1038 1038 |
5884 5884 |
439153 439153 |
887 887 |
22247451 962 22247451 962 |
5886 5886 |
5893 5893 |
||||||
| 1fyzA |
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Bound:2xFE2 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fyzB |
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Bound:2xFE2 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz0A |
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Bound:2xFE2 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz0B |
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Bound:2xFE2 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz1A |
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Bound:2x_FE | Unbound | Unbound | Unbound | Unbound | Analogue:FMT | Unbound | Unbound | |||
| 1fz1B |
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Bound:2x_FE | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz2A |
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Bound:2xFE2 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz2B |
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Bound:2xFE2 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz3A |
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Bound:2x_FE | Unbound | Unbound | Unbound | Unbound | Analogue:FMT | Unbound | Unbound | |||
| 1fz3B |
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Bound:2x_FE | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz4A |
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Bound:2x_FE | Unbound | Unbound | Unbound | Unbound | Analogue:FMT | Unbound | Unbound | |||
| 1fz4B |
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Bound:2x_FE | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz5A |
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Bound:FE2 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz5B |
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Bound:FE2 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz7A |
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Bound:2x_FE | Unbound | Unbound | Unbound | Unbound | Analogue:FMT | Unbound | Unbound | |||
| 1fz7B |
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Bound:2x_FE | Unbound | Unbound | Unbound | Unbound | Analogue:EOH | Unbound | Unbound | |||
| 1mhyD |
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Bound:2x_FE | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mhzD |
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Bound:2x_FE | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mmoD |
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Bound:2x_FE | Unbound | Unbound | Unbound | Unbound | Analogue:ACY | Unbound | Unbound | |||
| 1mmoE |
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Bound:2x_FE | Unbound | Unbound | Unbound | Unbound | Analogue:ACY | Unbound | Unbound | |||
| 1mtyD |
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Bound:2x_FE | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mtyE |
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Bound:2x_FE | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fyzC |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fyzD |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz0C |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz0D |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz1C |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz1D |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz2C |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz2D |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz3C |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz3D |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz4C |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz4D |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz5C |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz5D |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz7C |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz7D |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mhyB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mhzB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mmoB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mmoC |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mtyB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mtyC |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fyzE01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fyzF01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz0E01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz0F01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz1E01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz1F01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz2E01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz2F01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz3E01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz3F01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz4E01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz4F01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz5E01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz5F01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz7E01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz7F01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mhyG01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mhzG01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mmoG01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mmoH01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mtyG01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mtyH01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fyzE02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fyzF02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz0E02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz0F02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz1E02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz1F02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz2E02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz2F02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz3E02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz3F02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz4E02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz4F02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz5E02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz5F02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz7E02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1fz7F02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mhyG02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mhzG02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mmoG02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mmoH02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mtyG02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1mtyH02 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;P22869, P27353 & literature [3], [7] & [8] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1fyzA |
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CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1fyzB |
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CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1fz0A |
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CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1fz0B |
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CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1fz1A |
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CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1fz1B |
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CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1fz2A |
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CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1fz2B |
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CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1fz3A |
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CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1fz3B |
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CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1fz4A |
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CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1fz4B |
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CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1fz5A |
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CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1fz5B |
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CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1fz7A |
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CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1fz7B |
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CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1mhyD |
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CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1mhzD |
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CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1mmoD |
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CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1mmoE |
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|
|
|
CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1mtyD |
|
|
|
|
|
CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1mtyE |
|
|
|
|
|
CYS 151;THR 213 | GLU 114;GLU 144;HIS 147(Iron-1 binding);GLU 209;GLU 243;HIS 246(Iron-2 binding) | |||
| 1fyzC |
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| 1fyzD |
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| 1fz0C |
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| 1fz0D |
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| 1fz1C |
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| 1fz1D |
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| 1fz2C |
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| 1fz2D |
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| 1fz3C |
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| 1fz3D |
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| 1fz4C |
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| 1fz4D |
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| 1fz5C |
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| 1fz5D |
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| 1fz7C |
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| 1fz7D |
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| 1mhyB |
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| 1mhzB |
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| 1mmoB |
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| 1mmoC |
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| 1mtyB |
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| 1mtyC |
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| 1fyzE01 |
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| 1fyzF01 |
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| 1fz0E01 |
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| 1fz0F01 |
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| 1fz1E01 |
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| 1fz1F01 |
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| 1fz2E01 |
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| 1fz2F01 |
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| 1fz3E01 |
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| 1fz3F01 |
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| 1fz4E01 |
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| 1fz4F01 |
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| 1fz5E01 |
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| 1fz5F01 |
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| 1fz7E01 |
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| 1fz7F01 |
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| 1mhyG01 |
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| 1mhzG01 |
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| 1mmoG01 |
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| 1mmoH01 |
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| 1mtyG01 |
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| 1mtyH01 |
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| 1fyzE02 |
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| 1fyzF02 |
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| 1fz0E02 |
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| 1fz0F02 |
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| 1fz1E02 |
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| 1fz1F02 |
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| 1fz2E02 |
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| 1fz2F02 |
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| 1fz3E02 |
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| 1fz3F02 |
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| 1fz4E02 |
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| 1fz4F02 |
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| 1fz5E02 |
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| 1fz5F02 |
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| 1fz7E02 |
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| 1fz7F02 |
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| 1mhyG02 |
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| 1mhzG02 |
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| 1mmoG02 |
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| 1mmoH02 |
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| 1mtyG02 |
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| 1mtyH02 |
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|||||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[3]
|
Fig.3 | |
|
[4]
|
SCHEME 1, p.17596 | 4 |
|
[6]
|
SCHEME 1, SCHEME 2 | 6 |
|
[7]
|
p.541 | |
|
[8]
|
Fig.6, p.412-416 | |
|
[10]
|
Fig.1,p.65-67 | 5 |
|
[11]
|
Fig.1, Fig.8, p.5232-5233 | 7 |
|
[13]
|
Fig.1, p.560-562 | 7 |
|
[14]
|
p.143-147 | |
|
[15]
|
Scheme 1 | 4 |
|
[18]
|
Scheme 2, Scheme 4 | 4 |
|
[19]
|
Scheme 4, p.4430-4431 | 3 |
|
[21]
|
Fig.5, p.10774-10776 | |
|
[23]
|
Scheme 1 | 7 |
|
[24]
|
Fig.2 | 4 |
|
[25]
|
Fig.1, p.28 | 5 |
|
[25]
|
Scheme 2 | 4 |
|
[26]
|
Scheme 1 | 7 |
|
[28]
|
p.831-835 | |
|
[29]
|
p.1795 | |
|
[37]
|
Fig.7, p.71-73 | |
| References | |
|---|---|
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| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2840063 |
| Journal | Biochem Biophys Res Commun |
| Year | 1988 |
| Volume | 154 |
| Pages | 165-70 |
| Authors | Fox BG, Lipscomb JD |
| Title | Purification of a high specific activity methane monooxygenase hydroxylase component from a type II methanotroph. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2542319 |
| Journal | J Biol Chem |
| Year | 1989 |
| Volume | 264 |
| Pages | 10023-33 |
| Authors | Fox BG, Froland WA, Dege JE, Lipscomb JD |
| Title |
Methane monooxygenase from Methylosinus trichosporium OB3b. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1644180 |
| Journal | FEBS Lett |
| Year | 1992 |
| Volume | 307 |
| Pages | 257-62 |
| Authors | Nordlund P, Dalton H, Eklund H |
| Title | The active site structure of methane monooxygenase is closely related to the binuclear iron center of ribonucleotide reductase. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1325441 |
| Journal | J Biol Chem |
| Year | 1992 |
| Volume | 267 |
| Pages | 17588-97 |
| Authors | Froland WA, Andersson KK, Lee SK, Liu Y, Lipscomb JD |
| Title |
Methane monooxygenase component B and reductase alter the regioselectivity of the hydroxylase component-catalyzed reactions. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8223558 |
| Journal | Eur J Biochem |
| Year | 1993 |
| Volume | 217 |
| Pages | 217-23 |
| Authors | Atta M, Fontecave M, Wilkins PC, Dalton H |
| Title | Abduction of iron(III) from the soluble methane monooxygenase hydroxylase and reconstitution of the binuclear site with iron and manganese. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8408008 |
| Journal | J Biol Chem |
| Year | 1993 |
| Volume | 268 |
| Pages | 21569-77 |
| Authors | Lee SK, Nesheim JC, Lipscomb JD |
| Title | Transient intermediates of the methane monooxygenase catalytic cycle. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). |
| Medline ID | 94077176 |
| PubMed ID | 8255292 |
| Journal | Nature |
| Year | 1993 |
| Volume | 366 |
| Pages | 537-43 |
| Authors | Rosenzweig AC, Frederick CA, Lippard SJ, Nordlund P |
| Title | Crystal structure of a bacterial non-haem iron hydroxylase that catalyses the biological oxidation of methane. |
| Related PDB | 1mmo |
| Related UniProtKB | P22869 P18798 P11987 |
| [8] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). |
| Medline ID | 98092034 |
| PubMed ID | 9432288 |
| Journal | Chem Biol |
| Year | 1995 |
| Volume | 2 |
| Pages | 409-18 |
| Authors | Rosenzweig AC, Nordlund P, Takahara PM, Frederick CA, Lippard SJ |
| Title | Geometry of the soluble methane monooxygenase catalytic diiron center in two oxidation states. |
| Related PDB | |
| Related UniProtKB | P22869 |
| [9] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | |
| Journal | J Inorg Biochem |
| Year | 1995 |
| Volume | 58 |
| Pages | 235-44 |
| Authors | Semrau JD, Zolandz D, Lidstrom ME, Chan SI |
| Title |
The role of copper in the pMMO of Methylococcus capsulatus bath: a structural vs. |
| Related PDB | |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9056845 |
| Journal | Biochem Soc Trans |
| Year | 1997 |
| Volume | 25 |
| Pages | 65-9 |
| Authors | Fontecave M, Menage S, Duboc-Toia C, Vincent JM, Lambeaux C |
| Title | Model complexes of di-iron sites in methane mono-oxygenase and ribonucleotide reductase: structure and reactivity. |
| Related PDB | |
| Related UniProtKB | |
| [11] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9136884 |
| Journal | Biochemistry |
| Year | 1997 |
| Volume | 36 |
| Pages | 5223-33 |
| Authors | Liu Y, Nesheim JC, Paulsen KE, Stankovich MT, Lipscomb JD |
| Title | Roles of the methane monooxygenase reductase component in the regulation of catalysis. |
| Related PDB | |
| Related UniProtKB | |
| [12] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9054392 |
| Journal | J Biol Chem |
| Year | 1997 |
| Volume | 272 |
| Pages | 7022-6 |
| Authors | Davydov A, Davydov R, Graslund A, Lipscomb JD, Andersson KK |
| Title | Radiolytic reduction of methane monooxygenase dinuclear iron cluster at 77 K.@EPR evidence for conformational change upon reduction or binding of component B to the diferric state. |
| Related PDB | |
| Related UniProtKB | |
| [13] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 9070438 |
| Journal | Protein Sci |
| Year | 1997 |
| Volume | 6 |
| Pages | 556-68 |
| Authors | Elango N, Radhakrishnan R, Froland WA, Wallar BJ, Earhart CA, Lipscomb JD, Ohlendorf DH |
| Title | Crystal structure of the hydroxylase component of methane monooxygenase from Methylosinus trichosporium OB3b. |
| Related PDB | 1mhy 1mhz |
| Related UniProtKB | |
| [14] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). |
| Medline ID | 97469634 |
| PubMed ID | 9329079 |
| Journal | Proteins |
| Year | 1997 |
| Volume | 29 |
| Pages | 141-52 |
| Authors | Rosenzweig AC, Brandstetter H, Whittington DA, Nordlund P, Lippard SJ, Frederick CA |
| Title | Crystal structures of the methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath): implications for substrate gating and component interactions. |
| Related PDB | 1mty |
| Related UniProtKB | P22869 |
| [15] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8999792 |
| Journal | Science |
| Year | 1997 |
| Volume | 275 |
| Pages | 515-8 |
| Authors | Shu L, Nesheim JC, Kauffmann K, Munck E, Lipscomb JD, Que L Jr |
| Title | An Fe2IVO2 diamond core structure for the key intermediate Q of methane monooxygenase. |
| Related PDB | |
| Related UniProtKB | |
| [16] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10231531 |
| Journal | Biochemistry |
| Year | 1999 |
| Volume | 38 |
| Pages | 5799-812 |
| Authors | Chang SL, Wallar BJ, Lipscomb JD, Mayo KH |
| Title | Solution structure of component B from methane monooxygenase derived through heteronuclear NMR and molecular modeling. |
| Related PDB | |
| Related UniProtKB | |
| [17] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10346895 |
| Journal | Biochemistry |
| Year | 1999 |
| Volume | 38 |
| Pages | 6752-60 |
| Authors | Gallagher SC, Callaghan AJ, Zhao J, Dalton H, Trewhella J |
| Title | Global conformational changes control the reactivity of methane monooxygenase. |
| Related PDB | |
| Related UniProtKB | |
| [18] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10504247 |
| Journal | Biochemistry |
| Year | 1999 |
| Volume | 38 |
| Pages | 12768-85 |
| Authors | Gassner GT, Lippard SJ |
| Title | Component interactions in the soluble methane monooxygenase system from Methylococcus capsulatus (Bath). |
| Related PDB | |
| Related UniProtKB | |
| [19] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10194363 |
| Journal | Biochemistry |
| Year | 1999 |
| Volume | 38 |
| Pages | 4423-32 |
| Authors | Lee SK, Lipscomb JD |
| Title | Oxygen activation catalyzed by methane monooxygenase hydroxylase component: proton delivery during the O-O bond cleavage steps. |
| Related PDB | |
| Related UniProtKB | |
| [20] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10381404 |
| Journal | Chem Biol |
| Year | 1999 |
| Volume | 6 |
| Pages | 441-9 |
| Authors | Brandstetter H, Whittington DA, Lippard SJ, Frederick CA |
| Title | Mutational and structural analyses of the regulatory protein B of soluble methane monooxygenase from Methylococcus capsulatus (Bath). |
| Related PDB | |
| Related UniProtKB | |
| [21] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10196150 |
| Journal | J Biol Chem |
| Year | 1999 |
| Volume | 274 |
| Pages | 10771-6 |
| Authors | Valentine AM, LeTadic-Biadatti MH, Toy PH, Newcomb M, Lippard SJ |
| Title | Oxidation of ultrafast radical clock substrate probes by the soluble methane monooxygenase from Methylococcus capsulatus (Bath). |
| Related PDB | |
| Related UniProtKB | |
| [22] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10393915 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 1999 |
| Volume | 96 |
| Pages | 7877-82 |
| Authors | Walters KJ, Gassner GT, Lippard SJ, Wagner G |
| Title | Structure of the soluble methane monooxygenase regulatory protein B. |
| Related PDB | |
| Related UniProtKB | |
| [23] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11063587 |
| Journal | Biochemistry |
| Year | 2000 |
| Volume | 39 |
| Pages | 13503-15 |
| Authors | Brazeau BJ, Lipscomb JD |
| Title | Kinetics and activation thermodynamics of methane monooxygenase compound Q formation and reaction with substrates. |
| Related PDB | |
| Related UniProtKB | |
| [24] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10742188 |
| Journal | Curr Opin Chem Biol |
| Year | 2000 |
| Volume | 4 |
| Pages | 235-41 |
| Authors | Westerheide L, Pascaly M, Krebs B |
| Title | Methane monooxygenase and its related biomimetic models. |
| Related PDB | |
| Related UniProtKB | |
| [25] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10714702 |
| Journal | J Inorg Biochem |
| Year | 2000 |
| Volume | 78 |
| Pages | 23-34 |
| Authors | Yoshizawa K |
| Title | Two-step concerted mechanism for methane hydroxylation on the diiron active site of soluble methane monooxygenase. |
| Related PDB | |
| Related UniProtKB | |
| [26] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11329291 |
| Journal | Biochemistry |
| Year | 2001 |
| Volume | 40 |
| Pages | 2220-33 |
| Authors | Wallar BJ, Lipscomb JD |
| Title | Methane monooxygenase component B mutants alter the kinetics of steps throughout the catalytic cycle. |
| Related PDB | |
| Related UniProtKB | |
| [27] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11459514 |
| Journal | J Am Chem Soc |
| Year | 2001 |
| Volume | 123 |
| Pages | 7194-5 |
| Authors | White MC, Doyle AG, Jacobsen EN |
| Title |
A synthetically useful, |
| Related PDB | |
| Related UniProtKB | |
| [28] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS). |
| Medline ID | 21350666 |
| PubMed ID | 11456616 |
| Journal | J Am Chem Soc |
| Year | 2001 |
| Volume | 123 |
| Pages | 827-38 |
| Authors | Whittington DA, Lippard SJ |
| Title | Crystal structures of the soluble methane monooxygenase hydroxylase from Methylococcus capsulatus (Bath) demonstrating geometrical variability at the dinuclear iron active site. |
| Related PDB | 1fyz 1fz0 1fz1 1fz2 1fz3 1fz4 1fz5 |
| Related UniProtKB | P22869 |
| [29] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 11456795 |
| Journal | J Am Chem Soc |
| Year | 2001 |
| Volume | 123 |
| Pages | 1794-5 |
| Authors | Whittington DA, Sazinsky MH, Lippard SJ |
| Title | X-ray crystal structure of alcohol products bound at the active site of soluble methane monooxygenase hydroxylase. |
| Related PDB | 1fz7 |
| Related UniProtKB | |
| [30] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11851404 |
| Journal | Biochemistry |
| Year | 2002 |
| Volume | 41 |
| Pages | 2571-9 |
| Authors | Balendra S, Lesieur C, Smith TJ, Dalton H |
| Title | Positively charged amino acids are essential for electron transfer and protein-protein interactions in the soluble methane monooxygenase complex from Methylococcus capsulatus (Bath). |
| Related PDB | |
| Related UniProtKB | |
| [31] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11772001 |
| Journal | Biochemistry |
| Year | 2002 |
| Volume | 41 |
| Pages | 42-51 |
| Authors | Muller J, Lugovskoy AA, Wagner G, Lippard SJ |
| Title | NMR structure of the [2Fe-2S] ferredoxin domain from soluble methane monooxygenase reductase and interaction with its hydroxylase. |
| Related PDB | |
| Related UniProtKB | |
| [32] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11952785 |
| Journal | Eur J Biochem |
| Year | 2002 |
| Volume | 269 |
| Pages | 1835-43 |
| Authors | Callaghan AJ, Smith TJ, Slade SE, Dalton H |
| Title | Residues near the N-terminus of protein B control autocatalytic proteolysis and the activity of soluble methane mono-oxygenase. |
| Related PDB | |
| Related UniProtKB | |
| [33] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11849083 |
| Journal | Inorg Chem |
| Year | 2002 |
| Volume | 41 |
| Pages | 827-37 |
| Authors | Lee D, Lippard SJ |
| Title | Synthetic analogue of the [Fe(2)(mu-OH)(2)(mu-O(2)CR)](3+) core of soluble methane monooxygenase hydroxylase via synthesis and dioxygen reactivity of carboxylate-bridged diiron(II) complexes. |
| Related PDB | |
| Related UniProtKB | |
| [34] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11942853 |
| Journal | J Am Chem Soc |
| Year | 2002 |
| Volume | 124 |
| Pages | 4135-48 |
| Authors | Musaev DG, Basch H, Morokuma K |
| Title |
Theoretical study of the mechanism of alkane hydroxylation and ethylene epoxidation reactions catalyzed by diiron bis-oxo complexes. |
| Related PDB | |
| Related UniProtKB | |
| [35] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12059209 |
| Journal | J Am Chem Soc |
| Year | 2002 |
| Volume | 124 |
| Pages | 6879-86 |
| Authors | Newcomb M, Shen R, Lu Y, Coon MJ, Hollenberg PF, Kopp DA, Lippard SJ |
| Title | Evaluation of norcarane as a probe for radicals in cytochome p450- and soluble methane monooxygenase-catalyzed hydroxylation reactions. |
| Related PDB | |
| Related UniProtKB | |
| [36] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11890772 |
| Journal | J Am Chem Soc |
| Year | 2002 |
| Volume | 124 |
| Pages | 2416-7 |
| Authors | Tshuva EY, Lee D, Bu W, Lippard SJ |
| Title | Catalytic oxidation by a carboxylate-bridged non-heme diiron complex. |
| Related PDB | |
| Related UniProtKB | |
| [37] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11913390 |
| Journal | J Comput Chem |
| Year | 2002 |
| Volume | 23 |
| Pages | 59-76 |
| Authors | Torrent M, Musaev DG, Basch H, Morokuma K |
| Title | Computational studies of reaction mechanisms of methane monooxygenase and ribonucleotide reductase. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme, Whilst the component B (MMOB) is a regulatory unit of this enzyme by interacting with alpha chains of the component A, This entry corresponds to the component A (MMOH). This enzyme catalyzes the following reactions: (A) Oxygenation of methane (CH4) by O2, (B) Reduction of dinuclear iron site by NAD(P)H: |
| Created | Updated |
|---|---|
| 2004-07-29 | 2009-02-26 |