DB code: M00164
| CATH domain | -.-.-.- : | |
|---|---|---|
| 2.40.30.10 : Elongation Factor Tu (Ef-tu); domain 3 | ||
| 1.20.990.10 : NADPH-cytochrome p450 Reductase; Chain A, domain 3 | ||
| 3.40.50.80 : Rossmann fold | ||
| -.-.-.- : | ||
| 3.30.413.10 : Sulfite Reductase Hemoprotein; domain 1 | Catalytic domain | |
| 3.90.480.10 : Sulfite Reductase Hemoprotein; domain 2 | Catalytic domain | |
| 3.30.413.10 : Sulfite Reductase Hemoprotein; domain 1 | Catalytic domain | |
| E.C. | 1.8.1.2 | |
| CSA | 1aop | |
| M-CSA | 1aop | |
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 1.20.990.10 : NADPH-cytochrome p450 Reductase; Chain A, domain 3 | M00006 |
| 2.40.30.10 : Elongation Factor Tu (Ef-tu); domain 3 | D00043 M00006 M00141 M00159 |
| 3.40.50.80 : Rossmann fold | D00043 M00006 M00141 M00159 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| P38038 |
Sulfite reductase [NADPH] flavoprotein alpha-component
|
SIR-FP
EC 1.8.1.2 |
NP_417244.1
(Protein)
NC_000913.2 (DNA/RNA sequence) YP_490973.1 (Protein) NC_007779.1 (DNA/RNA sequence) |
PF00667
(FAD_binding_1)
PF00258 (Flavodoxin_1) PF00175 (NAD_binding_1) [Graphical View] |
| P17846 |
Sulfite reductase [NADPH] hemoprotein beta-component
|
SIR-HP
SIRHP EC 1.8.1.2 |
NP_417243.1
(Protein)
NC_000913.2 (DNA/RNA sequence) YP_490972.1 (Protein) NC_007779.1 (DNA/RNA sequence) |
PF01077
(NIR_SIR)
PF03460 (NIR_SIR_ferr) [Graphical View] |
| KEGG enzyme name |
|---|
|
sulfite reductase (NADPH)
sulfite (reduced nicotinamide adenine dinucleotide phosphate)reductase NADPH-sulfite reductase NADPH-dependent sulfite reductase H2S-NADP oxidoreductase sulfite reductase (NADPH2) |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P38038 | CYSJ_ECOLI | H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH. | Alpha(8)-beta(8). The alpha component is a flavoprotein, the beta component is a hemoprotein. | Binds 1 FAD per subunit. Binds 1 FMN per subunit. | |
| P17846 | CYSI_ECOLI | H(2)S + 3 NADP(+) + 3 H(2)O = sulfite + 3 NADPH. | Alpha(8)-beta(4). The alpha component is a flavoprotein, the beta component is a hemoprotein. | Binds 1 siroheme per subunit. Binds 1 4Fe-4S cluster per subunit. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00920 | Sulfur metabolism |
| Compound table | ||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | |||||||||||||
| KEGG-id | L00024 | C00748 | C00016 | C00061 | C00094 | C00005 | C00080 | C00283 | C00006 | C00001 | ||||||
| E.C. | ||||||||||||||||
| Compound | [4Fe-4S] | Siroheme | FAD | FMN | Sulfite | NADPH | H+ | Hydrogen sulfide | NADP+ | H2O | ||||||
| Type | heavy metal,sulfide group | aromatic ring (with nitrogen atoms),carboxyl group,heavy metal | amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide | amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,phosphate group/phosphate ion | sulfite | amide group,amine group,nucleotide | others | sulfhydryl group | amide group,amine group,nucleotide | H2O | ||||||
| ChEBI |
33725 33725 |
28599 28599 |
16238 16238 |
17621 17621 |
48854 48854 |
16474 16474 |
15378 15378 |
16136 16136 |
18009 18009 |
15377 15377 |
||||||
| PubChem |
25199933 439303 5460009 9548568 25199933 439303 5460009 9548568 |
643975 643975 |
643976 643976 |
1100 22132154 1100 22132154 |
5884 5884 |
1038 1038 |
18779926 402 18779926 402 |
5886 5886 |
22247451 962 22247451 962 |
|||||||
| 1ddgA01 |
|
|
|
|
|
Unbound | Unbound | Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ddgB01 |
|
|
|
|
|
Unbound | Unbound | Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ddiA01 |
|
|
|
|
|
Unbound | Unbound | Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ddgA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ddgB02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ddiA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ddgA03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ddgB03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ddiA03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Bound:NAP | Unbound | Unbound | Unbound | ||
| 1aopA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Analogue:PO4 | Unbound | Unbound | Unbound | Unbound | ||
| 1geoA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Analogue:PO4 | Unbound | Unbound | Unbound | Unbound | ||
| 1gepA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Bound:SO3 | Unbound | Unbound | Unbound | Unbound | ||
| 2aopA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Analogue:PO4 | Unbound | Unbound | Unbound | Unbound | ||
| 2gepA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Bound:SO3 | Unbound | Unbound | Unbound | Unbound | ||
| 3aopA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Analogue:PO4 | Unbound | Unbound | Unbound | Unbound | ||
| 3geoA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-bound:NO2 | ||
| 4aopA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Analogue:PO4 | Unbound | Unbound | Unbound | Unbound | ||
| 4gepA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:CYN | ||
| 5aopA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 5gepA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:CMO | ||
| 6gepA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:_NO | ||
| 7gepA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-bound:_SX | ||
| 8gepA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1aopA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1geoA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1gepA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2aopA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2gepA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 3aopA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 3geoA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 4aopA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 4gepA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 5aopA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 5gepA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 6gepA02 |
|
|
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|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 7gepA02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 8gepA02 |
|
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|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1aopA03 |
|
|
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|
|
Bound:SF4 | Bound:SRM-PO4 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1geoA03 |
|
|
|
|
|
Bound:FS4 | Bound:SRM-PO4 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1gepA03 |
|
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|
Bound:FS4 | Bound:SRM-SO3 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2aopA03 |
|
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Bound:SF4 | Bound:SRM-PO4 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 2gepA03 |
|
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Bound:SF4 | Bound:SRM-SO3 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 3aopA03 |
|
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Bound:SF4 | Bound:SRM-PO4 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 3geoA03 |
|
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Bound:SF4 | Bound:SRM-NO2 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 4aopA03 |
|
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Bound:SF4 | Bound:SRM-PO4 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 4gepA03 |
|
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Bound:SF4 | Bound:SRM-CYN | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 5aopA03 |
|
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Bound:SF4 | Bound:SRM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 5gepA03 |
|
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Bound:SF4 | Bound:SRM-CMO | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 6gepA03 |
|
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Bound:SF4 | Bound:SRM-_NO | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 7gepA03 |
|
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Bound:SF4 | Bound:SRM-_SX | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 8gepA03 |
|
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|
Bound:SF4 | Bound:SRM | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;P17846 & PDB;1aop & literature [14], [15] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1ddgA01 |
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| 1ddgB01 |
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| 1ddiA01 |
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| 1ddgA02 |
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|||||
| 1ddgB02 |
|
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|||||
| 1ddiA02 |
|
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|||||
| 1ddgA03 |
|
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|||||
| 1ddgB03 |
|
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| 1ddiA03 |
|
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|||||
| 1aopA01 |
|
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ARG 153;LYS 215;LYS 217 | ||||
| 1geoA01 |
|
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ARG 153;LYS 215;LYS 217 | ||||
| 1gepA01 |
|
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ARG 153;LYS 215;LYS 217 | ||||
| 2aopA01 |
|
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|
|
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ARG 153;LYS 215;LYS 217 | ||||
| 2gepA01 |
|
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ARG 153;LYS 215;LYS 217 | ||||
| 3aopA01 |
|
|
|
|
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ARG 153;LYS 215;LYS 217 | ||||
| 3geoA01 |
|
|
|
|
|
ARG 153;LYS 215;LYS 217 | ||||
| 4aopA01 |
|
|
|
|
|
ARG 153;LYS 215;LYS 217 | ||||
| 4gepA01 |
|
|
|
|
|
ARG 153;LYS 215;LYS 217 | ||||
| 5aopA01 |
|
|
|
|
|
ARG 153;LYS 215;LYS 217 | ||||
| 5gepA01 |
|
|
|
|
|
ARG 153;LYS 215;LYS 217 | ||||
| 6gepA01 |
|
|
|
|
|
ARG 153;LYS 215;LYS 217 | ||||
| 7gepA01 |
|
|
|
|
|
ARG 153;LYS 215;LYS 217 | ||||
| 8gepA01 |
|
|
|
|
|
ARG 153;LYS 215;LYS 217 | ||||
| 1aopA02 |
|
|
|
|
|
ARG 83 | ||||
| 1geoA02 |
|
|
|
|
|
ARG 83 | ||||
| 1gepA02 |
|
|
|
|
|
ARG 83 | ||||
| 2aopA02 |
|
|
|
|
|
ARG 83 | ||||
| 2gepA02 |
|
|
|
|
|
ARG 83 | ||||
| 3aopA02 |
|
|
|
|
|
ARG 83 | ||||
| 3geoA02 |
|
|
|
|
|
ARG 83 | ||||
| 4aopA02 |
|
|
|
|
|
ARG 83 | ||||
| 4gepA02 |
|
|
|
|
|
ARG 83 | ||||
| 5aopA02 |
|
|
|
|
|
ARG 83 | ||||
| 5gepA02 |
|
|
|
|
|
ARG 83 | ||||
| 6gepA02 |
|
|
|
|
|
ARG 83 | ||||
| 7gepA02 |
|
|
|
|
|
ARG 83 | ||||
| 8gepA02 |
|
|
|
|
|
ARG 83 | ||||
| 1aopA03 |
|
|
|
|
|
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding) | ||||
| 1geoA03 |
|
|
|
|
|
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding) | ||||
| 1gepA03 |
|
|
|
|
|
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding) | ||||
| 2aopA03 |
|
|
|
|
|
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding) | ||||
| 2gepA03 |
|
|
|
|
|
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding) | ||||
| 3aopA03 |
|
|
|
|
|
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding) | ||||
| 3geoA03 |
|
|
|
|
|
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding) | ||||
| 4aopA03 |
|
|
|
|
|
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding) | ||||
| 4gepA03 |
|
|
|
|
|
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding) | ||||
| 5aopA03 |
|
|
|
|
|
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding) | ||||
| 5gepA03 |
|
|
|
|
|
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding) | ||||
| 6gepA03 |
|
|
|
|
|
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding) | ||||
| 7gepA03 |
|
|
|
|
|
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding) | ||||
| 8gepA03 |
|
|
|
|
|
CYS 434;CYS 440;CYS 479;CYS 483(4Fe-4S binding);CYS 483(Siroheme binding) | ||||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[5]
|
Scheme 1, p.15805-15806 | |
|
[8]
|
p.18607-18608 | |
|
[9]
|
p.64-66 | |
|
[12]
|
Scheme 1, p.20554-20555 | |
|
[13]
|
||
|
[14]
|
p.12114-12118 | |
|
[15]
|
Fig.13, 12133-12126 | |
|
[17]
|
Scheme 2, Scheme 3, p.6120-6122 | |
|
[18]
|
Scheme 1 | |
|
[21]
|
||
|
[22]
|
||
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 6281269 |
| Journal | J Biol Chem |
| Year | 1982 |
| Volume | 257 |
| Pages | 6343-50 |
| Authors | Siegel LM, Rueger DC, Barber MJ, Krueger RJ, Orme-Johnson NR, Orme-Johnson WH |
| Title |
Escherichia coli sulfite reductase hemoprotein subunit. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 3525540 |
| Journal | J Biol Chem |
| Year | 1986 |
| Volume | 261 |
| Pages | 10277-81 |
| Authors | McRee DE, Richardson DC, Richardson JS, Siegel LM |
| Title | The heme and Fe4S4 cluster in the crystallographic structure of Escherichia coli sulfite reductase. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 3056517 |
| Journal | Biochemistry |
| Year | 1988 |
| Volume | 27 |
| Pages | 5984-90 |
| Authors | Young LJ, Siegel LM |
| Title | Superoxidized states of Escherichia coli sulfite reductase heme protein subunit. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2670946 |
| Journal | J Biol Chem |
| Year | 1989 |
| Volume | 264 |
| Pages | 15726-37 |
| Authors | Ostrowski J, Wu JY, Rueger DC, Miller BE, Siegel LM, Kredich NM |
| Title |
Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2550423 |
| Journal | J Biol Chem |
| Year | 1989 |
| Volume | 264 |
| Pages | 15796-808 |
| Authors | Ostrowski J, Barber MJ, Rueger DC, Miller BE, Siegel LM, Kredich NM |
| Title |
Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8457551 |
| Journal | Biochemistry |
| Year | 1993 |
| Volume | 32 |
| Pages | 2853-67 |
| Authors | Kaufman J, Spicer LD, Siegel LM |
| Title | Proton NMR of Escherichia coli sulfite reductase: the unligated hemeprotein subunit. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8395881 |
| Journal | Biochemistry |
| Year | 1993 |
| Volume | 32 |
| Pages | 8782-91 |
| Authors | Kaufman J, Siegel LM, Spicer LD |
| Title | Proton NMR of Escherichia coli sulfite reductase: studies of the heme protein subunit with added ligands. |
| Related PDB | |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8360156 |
| Journal | J Biol Chem |
| Year | 1993 |
| Volume | 268 |
| Pages | 18604-9 |
| Authors | Coves J, Niviere V, Eschenbrenner M, Fontecave M |
| Title |
NADPH-sulfite reductase from Escherichia coli. |
| Related PDB | |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7928966 |
| Journal | J Bacteriol |
| Year | 1994 |
| Volume | 176 |
| Pages | 6050-8 |
| Authors | Hansen J, Cherest H, Kielland-Brandt MC |
| Title |
Two divergent MET10 genes, |
| Related PDB | |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) |
| Medline ID | 96008578 |
| PubMed ID | 7569952 |
| Journal | Science |
| Year | 1995 |
| Volume | 270 |
| Pages | 59-67 |
| Authors | Crane BR, Siegel LM, Getzoff ED |
| Title | Sulfite reductase structure at 1.6 A: evolution and catalysis for reduction of inorganic anions. |
| Related PDB | 1aop 1geo 1gep |
| Related UniProtKB | P17846 |
| [11] | |
| Resource | |
| Comments | CHARACTERIZATION OF FAD AND FMN DOMAINS. |
| Medline ID | 96049560 |
| PubMed ID | 7589518 |
| Journal | FEBS Lett |
| Year | 1995 |
| Volume | 374 |
| Pages | 82-4 |
| Authors | Eschenbrenner M, Coves J, Fontecave M |
| Title | NADPH-sulfite reductase flavoprotein from Escherichia coli: contribution to the flavin content and subunit interaction. |
| Related PDB | |
| Related UniProtKB | P38038 |
| [12] | |
| Resource | |
| Comments | CHARACTERIZATION AS A NADPH:FLAVIN OXIDOREDUCTASE. |
| Medline ID | 95386502 |
| PubMed ID | 7657631 |
| Journal | J Biol Chem |
| Year | 1995 |
| Volume | 270 |
| Pages | 20550-5 |
| Authors | Eschenbrenner M, Coves J, Fontecave M |
| Title |
The flavin reductase activity of the flavoprotein component of sulfite reductase from Escherichia coli. |
| Related PDB | |
| Related UniProtKB | P38038 |
| [13] | |
| Resource | |
| Comments | CHARACTERIZATION OF FMN DOMAIN 1-219. |
| Medline ID | 97297802 |
| PubMed ID | 9153434 |
| Journal | Biochemistry |
| Year | 1997 |
| Volume | 36 |
| Pages | 5921-8 |
| Authors | Coves J, Zeghouf M, Macherel D, Guigliarelli B, Asso M, Fontecave M |
| Title | Flavin mononucleotide-binding domain of the flavoprotein component of the sulfite reductase from Escherichia coli. |
| Related PDB | |
| Related UniProtKB | P38038 |
| [14] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) |
| Medline ID | 97461529 |
| PubMed ID | 9315848 |
| Journal | Biochemistry |
| Year | 1997 |
| Volume | 36 |
| Pages | 12101-19 |
| Authors | Crane BR, Siegel LM, Getzoff ED |
| Title | Structures of the siroheme- and Fe4S4-containing active center of sulfite reductase in different states of oxidation: heme activation via reduction-gated exogenous ligand exchange. |
| Related PDB | 2aop 2gep 3aop 3geo 4aop 4gep 5aop 5gep 6gep 7gep 8gep |
| Related UniProtKB | P17846 |
| [15] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9315849 |
| Journal | Biochemistry |
| Year | 1997 |
| Volume | 36 |
| Pages | 12120-37 |
| Authors | Crane BR, Siegel LM, Getzoff ED |
| Title |
Probing the catalytic mechanism of sulfite reductase by X-ray crystallography: structures of the Escherichia coli hemoprotein in complex with substrates, |
| Related PDB | |
| Related UniProtKB | |
| [16] | |
| Resource | |
| Comments | CHARACTERIZATION AS A NADPH-CYTOCHROME P450 REDUCTASE. |
| Medline ID | 98289576 |
| PubMed ID | 9618257 |
| Journal | Biochem Biophys Res Commun |
| Year | 1998 |
| Volume | 246 |
| Pages | 602-5 |
| Authors | Zeghouf M, Defaye G, Fontecave M, Coves J |
| Title | The flavoprotein component of the Escherichia coli sulfite reductase can act as a cytochrome P450c17 reductase. |
| Related PDB | |
| Related UniProtKB | P38038 |
| [17] | |
| Resource | |
| Comments | CHARACTERIZATION. |
| Medline ID | 98226652 |
| PubMed ID | 9558350 |
| Journal | Biochemistry |
| Year | 1998 |
| Volume | 37 |
| Pages | 6114-23 |
| Authors | Zeghouf M, Fontecave M, Macherel D, Coves J |
| Title |
The flavoprotein component of the Escherichia coli sulfite reductase: expression, |
| Related PDB | |
| Related UniProtKB | P38038 |
| [18] | |
| Resource | |
| Comments | CHARACTERIZATION OF FAD DOMAIN. |
| Medline ID | 99386679 |
| PubMed ID | 10455035 |
| Journal | Biochem J |
| Year | 1999 |
| Volume | 342 |
| Pages | 465-72 |
| Authors | Coves J, Lebrun C, Gervasi G, Dalbon P, Fontecave M |
| Title | Overexpression of the FAD-binding domain of the sulphite reductase flavoprotein component from Escherichia coli and its inhibition by iodonium diphenyl chloride. |
| Related PDB | |
| Related UniProtKB | P38038 |
| [19] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10215853 |
| Journal | Eur J Biochem |
| Year | 1999 |
| Volume | 261 |
| Pages | 430-7 |
| Authors | Evrard A, Zeghouf M, Fontecave M, Roby C, Coves J |
| Title | 31P nuclear magnetic resonance study of the flavoprotein component of the Escherichia coli sulfite reductase. |
| Related PDB | |
| Related UniProtKB | |
| [20] | |
| Resource | |
| Comments | QUATERNARY STRUCTURE. |
| Medline ID | 20545508 |
| PubMed ID | 10984484 |
| Journal | J Biol Chem |
| Year | 2000 |
| Volume | 275 |
| Pages | 37651-6 |
| Authors | Zeghouf M, Fontecave M, Coves J |
| Title | A simplifed functional version of the Escherichia coli sulfite reductase. |
| Related PDB | |
| Related UniProtKB | P38038 |
| [21] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 225-598. |
| Medline ID | 20328609 |
| PubMed ID | 10860732 |
| Journal | J Mol Biol |
| Year | 2000 |
| Volume | 299 |
| Pages | 199-212 |
| Authors | Gruez A, Pignol D, Zeghouf M, Coves J, Fontecave M, Ferrer JL, Fontecilla-Camps JC |
| Title | Four crystal structures of the 60 kDa flavoprotein monomer of the sulfite reductase indicate a disordered flavodoxin-like module. |
| Related PDB | 1ddi 1ddg |
| Related UniProtKB | P38038 |
| [22] | |
| Resource | |
| Comments | CHARACTERIZATION AND STRUCTURE BY NMR OF 52-219. |
| Medline ID | 21885835 |
| PubMed ID | 11888295 |
| Journal | Biochemistry |
| Year | 2002 |
| Volume | 41 |
| Pages | 3770-80 |
| Authors | Champier L, Sibille N, Bersch B, Brutscher B, Blackledge M, Coves J |
| Title |
Reactivity, |
| Related PDB | |
| Related UniProtKB | P38038 |
| Comments |
|---|
|
This enzyme is made of two subunits, In contrast, According to the literature [5], |
| Created | Updated |
|---|---|
| 2004-03-25 | 2009-02-26 |