DB code: M00179
| CATH domain | 3.40.462.10 : Vanillyl-alcohol Oxidase; Chain A, domain 3 | Catalytic domain |
|---|---|---|
| 3.30.43.10 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2 | ||
| 3.30.465.20 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3 | Catalytic domain | |
| 1.10.45.10 : Vanillyl-alcohol Oxidase; Chain A, domain 4 | Catalytic domain | |
| 1.10.760.10 : Cytochrome Bc1 Complex; Chain D, domain 2 | Catalytic domain | |
| E.C. | 1.17.99.1 | |
| CSA | 1dii | |
| M-CSA | 1dii | |
| MACiE | M0141 | |
| CATH domain | Related DB codes (homologues) |
|---|---|
| 1.10.45.10 : Vanillyl-alcohol Oxidase; Chain A, domain 4 | M00004 |
| 1.10.760.10 : Cytochrome Bc1 Complex; Chain D, domain 2 | D00055 D00498 |
| 3.30.43.10 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 2 | M00001 M00004 M00039 T00003 |
| 3.30.465.20 : Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase; domain 3 | M00001 M00004 |
| 3.40.462.10 : Vanillyl-alcohol Oxidase; Chain A, domain 3 | M00004 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Pfam |
|---|---|---|---|
| P09787 |
4-cresol dehydrogenase [hydroxylating] cytochrome c subunit
|
Flavocytochrome c
P-cresol methylhydroxylase cytochrome subunit |
[Graphical View] |
| P09788 |
4-cresol dehydrogenase [hydroxylating] flavoprotein subunit
|
EC
1.17.99.1
P-cresol methylhydroxylase PCMH |
PF02913
(FAD-oxidase_C)
PF01565 (FAD_binding_4) [Graphical View] |
| KEGG enzyme name |
|---|
|
4-cresol dehydrogenase (hydroxylating)
p-cresol-(acceptor) oxidoreductase (hydroxylating) p-cresol methylhydroxylase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P09787 | CY4C_PSEPU | Tetramer of two cytochrome subunits and two flavoprotein subunits. | |||
| P09788 | DH4C_PSEPU | 4-cresol + acceptor + H(2)O = 4- hydroxybenzaldehyde + reduced acceptor. | Tetramer of two cytochrome subunits and two flavoprotein subunits. | Binds 1 FAD covalently per subunit. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00622 | Toluene and xylene degradation |
| Compound table | ||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | |||||||||||
| KEGG-id | C00016 | C00524 | C01468 | C00028 | C00001 | C00633 | C00030 | |||||||
| E.C. | ||||||||||||||
| Compound | FAD | Cytochrome c | 4-Cresol | Acceptor | H2O | 4-Hydroxybenzaldehyde | Reduced acceptor | quinone-methide intermediate | 4-hydroxybenzyl alcohol | |||||
| Type | amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide | amide group,amine group,aromatic ring (with nitrogen atoms),carboxyl group,heavy metal,sulfide group | aromatic ring (only carbon atom) | others | H2O | aromatic ring (only carbon atom),carbohydrate | others | |||||||
| ChEBI |
16238 16238 |
17847 17847 |
15377 15377 |
17597 17597 |
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| PubChem |
643975 643975 |
2879 2879 |
22247451 962 22247451 962 |
126 126 |
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| 1diiA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1diiB01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1diqA01 |
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Unbound | Unbound | Bound:PCR | Unbound | Unbound | Unbound | |||
| 1diqB01 |
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Unbound | Unbound | Bound:PCR | Unbound | Unbound | Unbound | |||
| 1wveA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1wveB01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1wvfA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1diiA02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1diiB02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1diqA02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1diqB02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1wveA02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1wveB02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1wvfA02 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1diiA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1diiB03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1diqA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1diqB03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1wveA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1wveB03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1wvfA03 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1diiA04 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1diiB04 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1diqA04 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1diqB04 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1wveA04 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1wveB04 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1wvfA04 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||
| 1diiC |
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Unbound | Analogue:HEM | Unbound | Unbound | Unbound | Unbound | |||
| 1diiD |
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Unbound | Analogue:HEM | Unbound | Unbound | Unbound | Unbound | |||
| 1diqC |
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Unbound | Analogue:HEM | Unbound | Unbound | Unbound | Unbound | |||
| 1diqD |
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Unbound | Analogue:HEM | Unbound | Unbound | Unbound | Unbound | |||
| 1wveC |
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Unbound | Analogue:HEM | Unbound | Unbound | Unbound | Unbound | |||
| 1wveD |
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Unbound | Analogue:HEM | Unbound | Unbound | Unbound | Unbound | |||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;P09787, P09788 & literature [8] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1diiA01 |
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TYR 95 | ||||
| 1diiB01 |
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TYR 95 | ||||
| 1diqA01 |
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TYR 95 | ||||
| 1diqB01 |
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TYR 95 | ||||
| 1wveA01 |
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TYR 95 | ||||
| 1wveB01 |
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TYR 95 | ||||
| 1wvfA01 |
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TYR 95 | ||||
| 1diiA02 |
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| 1diiB02 |
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| 1diqA02 |
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| 1diqB02 |
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| 1wveA02 |
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| 1wveB02 |
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| 1wvfA02 |
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| 1diiA03 |
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GLU 380;GLU 427;HIS 436;TYR 473 | TYR 384(FAD binding) | |||
| 1diiB03 |
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GLU 380;GLU 427;HIS 436;TYR 473 | TYR 384(FAD binding) | |||
| 1diqA03 |
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GLU 380;GLU 427;HIS 436;TYR 473 | TYR 384(FAD binding) | |||
| 1diqB03 |
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GLU 380;GLU 427;HIS 436;TYR 473 | TYR 384(FAD binding) | |||
| 1wveA03 |
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GLU 380;GLU 427;HIS 436;TYR 473 | TYR 384(FAD binding) | |||
| 1wveB03 |
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GLU 380;GLU 427;HIS 436;TYR 473 | TYR 384(FAD binding) | |||
| 1wvfA03 |
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GLU 380;GLU 427;HIS 436;TYR 473 | TYR 384(FAD binding) | |||
| 1diiA04 |
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ARG 474 | ||||
| 1diiB04 |
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ARG 474 | ||||
| 1diqA04 |
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ARG 474 | ||||
| 1diqB04 |
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ARG 474 | ||||
| 1wveA04 |
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ARG 474 | ||||
| 1wveB04 |
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ARG 474 | ||||
| 1wvfA04 |
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ARG 474 | ||||
| 1diiC |
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HIS 619;MET 650(Heme binding) | ALA 649 | |||
| 1diiD |
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HIS 619;MET 650(Heme binding) | ALA 649 | |||
| 1diqC |
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HIS 619;MET 650(Heme binding) | ALA 649 | |||
| 1diqD |
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HIS 619;MET 650(Heme binding) | ALA 649 | |||
| 1wveC |
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HIS 619;MET 650(Heme binding) | ALA 649 | |||
| 1wveD |
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HIS 619;MET 650(Heme binding) | ALA 649 | |||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
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[5]
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Fig.5, p.31207 | |
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[8]
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Fig.1, Fig.12, p.367-371 | |
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[14]
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p.10543-10545 | |
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[15]
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Fig.1, p.2963 | 3 |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 4020868 |
| Journal | J Mol Biol |
| Year | 1985 |
| Volume | 183 |
| Pages | 517-8 |
| Authors | Shamala N, Lim LW, Mathews FS, McIntire W, Singer TP, Hopper DJ |
| Title |
Preliminary X-ray study of p-cresol methylhydroxylase (flavocytochrome c) from Pseudomonas putida N.C.I.B. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 3460064 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 1986 |
| Volume | 83 |
| Pages | 4646-9 |
| Authors | Bruice TC, Zipplies MF, Lee WA |
| Title |
The pH dependence of the mechanism of reaction of hydrogen peroxide with a nonaggregating, |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) |
| Medline ID | 91105087 |
| PubMed ID | 1846290 |
| Journal | Biochemistry |
| Year | 1991 |
| Volume | 30 |
| Pages | 238-47 |
| Authors | Mathews FS, Chen ZW, Bellamy HD, McIntire WS |
| Title | Three-dimensional structure of p-cresol methylhydroxylase (flavocytochrome c) from Pseudomonas putida at 3.0-A resolution. |
| Related PDB | |
| Related UniProtKB | P09787 P09788 |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1946360 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 1991 |
| Volume | 88 |
| Pages | 9463-7 |
| Authors | McLendon GL, Bagby S, Charman JA, Driscoll PC, McIntire WS, Mathews FS, Hill HA |
| Title | Subunit interactions change the heme active-site geometry in p-cresol methylhydroxylase. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8537385 |
| Journal | J Biol Chem |
| Year | 1995 |
| Volume | 270 |
| Pages | 31202-9 |
| Authors | Kim J, Fuller JH, Kuusk V, Cunane L, Chen ZW, Mathews FS, McIntire WS |
| Title | The cytochrome subunit is necessary for covalent FAD attachment to the flavoprotein subunit of p-cresol methylhydroxylase. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9514256 |
| Journal | Protein Sci |
| Year | 1998 |
| Volume | 7 |
| Pages | 7-20 |
| Authors | Mewies M, McIntire WS, Scrutton NS |
| Title | Covalent attachment of flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN) to enzymes: the current state of affairs. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10600124 |
| Journal | Biochemistry |
| Year | 1999 |
| Volume | 38 |
| Pages | 16620-8 |
| Authors | Engst S, Kuusk V, Efimov I, Cronin CN, McIntire WS |
| Title | Properties of p-cresol methylhydroxylase flavoprotein overproduced by Escherichia coli. |
| Related PDB | |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) |
| Medline ID | 20090938 |
| PubMed ID | 10623531 |
| Journal | J Mol Biol |
| Year | 2000 |
| Volume | 295 |
| Pages | 357-74 |
| Authors | Cunane LM, Chen ZW, Shamala N, Mathews FS, Cronin CN, McIntire WS |
| Title | Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism. |
| Related PDB | 1dii 1diq |
| Related UniProtKB | P09787 P09788 |
| [9] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11192725 |
| Journal | Subcell Biochem |
| Year | 2000 |
| Volume | 35 |
| Pages | 29-72 |
| Authors | Mathews FS, Cunane L, Durley RC |
| Title | Flavin electron transfer proteins. |
| Related PDB | |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11329284 |
| Journal | Biochemistry |
| Year | 2001 |
| Volume | 40 |
| Pages | 2155-66 |
| Authors | Efimov I, Cronin CN, McIntire WS |
| Title | Effects of noncovalent and covalent FAD binding on the redox and catalytic properties of p-cresol methylhydroxylase. |
| Related PDB | |
| Related UniProtKB | |
| [11] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11514662 |
| Journal | Protein Sci |
| Year | 2001 |
| Volume | 10 |
| Pages | 1712-28 |
| Authors | Dym O, Eisenberg D |
| Title | Sequence-structure analysis of FAD-containing proteins. |
| Related PDB | |
| Related UniProtKB | |
| [12] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12057198 |
| Journal | Structure (Camb) |
| Year | 2002 |
| Volume | 10 |
| Pages | 837-49 |
| Authors | Chen ZW, Matsushita K, Yamashita T, Fujii TA, Toyama H, Adachi O, Bellamy HD, Mathews FS |
| Title | Structure at 1.9 A resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5. |
| Related PDB | |
| Related UniProtKB | |
| [13] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15147198 |
| Journal | Biochemistry |
| Year | 2004 |
| Volume | 43 |
| Pages | 6138-48 |
| Authors | Efimov I, Cronin CN, Bergmann DJ, Kuusk V, McIntire WS |
| Title |
Insight into covalent flavinylation and catalysis from redox, |
| Related PDB | |
| Related UniProtKB | |
| [14] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15301551 |
| Journal | Biochemistry |
| Year | 2004 |
| Volume | 43 |
| Pages | 10532-46 |
| Authors | Efimov I, McIntire WS |
| Title | A study of the spectral and redox properties and covalent flavinylation of the flavoprotein component of p-cresol methylhydroxylase reconstituted with FAD analogues. |
| Related PDB | |
| Related UniProtKB | |
| [15] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 12614613 |
| Journal | J Mol Biol |
| Year | 2003 |
| Volume | 327 |
| Pages | 129-44 |
| Authors | Nichols CE, Ren J, Lamb HK, Hawkins AR, Stammers DK |
| Title | Ligand-induced conformational changes and a mechanism for domain closure in Aspergillus nidulans dehydroquinate synthase. |
| Related PDB | 1wve 1wvf |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme is composed of flavoprotein subunit and cytochrome c subunit with a heme group.
According to the literature [8], (A) Hydride transfer from substrate, (B) Electron transfer from the flavin of FAD to the heme iron of the cytochrome c subunit (2 x one electron transfer): (C) Addition of water to the methide carbon of the quinone-methide intermediate, (D) Hydride transfer from the intermediate, (E) Electron transfer from the flavin of FAD to the heme iron of the cytochrome c subunit (2 x one electron transfer): # Electrons, |
| Created | Updated |
|---|---|
| 2005-05-19 | 2009-02-26 |