DB code: M00007
CATH domain | 3.40.50.740 : Rossmann fold | |
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3.40.228.10 : Dimethylsulfoxide Reductase; domain 2 | Catalytic domain | |
3.90.55.10 : Dimethylsulfoxide Reductase; domain 3 | ||
2.40.40.20 : Barwin-like endoglucanases | ||
E.C. | 1.7.2.3 | |
CSA | 1tmo | |
M-CSA | 1tmo | |
MACiE |
CATH domain | Related DB codes (homologues) |
---|---|
2.40.40.20 : Barwin-like endoglucanases | S00101 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Pfam |
---|---|---|---|
O87948 |
Trimethylamine-N-oxide reductase
|
TMAO reductase
Trimethylamine oxidase EC 1.7.2.3 |
PF00384
(Molybdopterin)
PF01568 (Molydop_binding) [Graphical View] |
KEGG enzyme name |
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trimethylamine-N-oxide reductase (cytochrome c)
TMAO reductase TOR |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
O87948 | TORA_SHEMA | Trimethylamine + 2 (ferricytochrome c)-subunit + H(2)O = trimethylamine N-oxide + 2 (ferrocytochrome c)-subunit + 2 H(+). | Periplasm. |
KEGG Pathways | Map code | Pathways | E.C. |
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Compound table | |||||||||||||
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Cofactors | Substrates | Products | Intermediates | ||||||||||
KEGG-id | C00150 | C00126 | C01104 | C00080 | C00125 | C00565 | C00001 | ||||||
E.C. | |||||||||||||
Compound | Molybdenum | Ferrocytochrome c | Trimethylamine N-oxide | H+ | Ferricytochrome c | Trimethylamine | H2O | ||||||
Type | heavy metal | amide group,amine group,aromatic ring (with nitrogen atoms),carboxyl group,heavy metal,sulfide group | amine group | others | amide group,amine group,aromatic ring (with nitrogen atoms),carboxyl group,heavy metal,sulfide group | amine group | H2O | ||||||
ChEBI |
28685 28685 |
15724 15724 |
15378 15378 |
18139 18139 |
15377 15377 |
||||||||
PubChem |
23932 23932 |
1145 1145 |
1038 1038 |
1146 1146 |
22247451 962 22247451 962 |
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1tmoA01 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
1tmoA02 | Bound:2MO | Unbound | Unbound | Unbound | Unbound | ||||||||
1tmoA03 | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||||
1tmoA04 | Unbound | Unbound | Unbound | Unbound | Unbound |
Reference for Active-site residues | ||
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resource | references | E.C. |
PDB;1tmo |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1tmoA01 | ||||||||||
1tmoA02 | SER 149 (Molybdenum binding) | |||||||||
1tmoA03 | ||||||||||
1tmoA04 |
References for Catalytic Mechanism | ||
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References | Sections | No. of steps in catalysis |
References | |
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[1] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) |
Medline ID | 99033057 |
PubMed ID | 9813128 |
Journal | J Mol Biol |
Year | 1998 |
Volume | 284 |
Pages | 435-47 |
Authors | Czjzek M, Dos Santos JP, Pommier J, Giordano G, Mejean V, Haser R |
Title | Crystal structure of oxidized trimethylamine N-oxide reductase from Shewanella massilia at 2.5 A resolution. |
Related PDB | 1tmo |
Related UniProtKB | O87948 |
[2] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11781311 |
Journal | J Biol Chem |
Year | 2002 |
Volume | 277 |
Pages | 10362-6 |
Authors | Allen SC, Barrett CM, Ray N, Robinson C |
Title | Essential cytoplasmic domains in the Escherichia coli TatC protein. |
Related PDB | |
Related UniProtKB |
Comments |
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Created | Updated |
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2004-03-25 | 2009-02-26 |