ID D6J8W3_ECOLX Unreviewed; 848 AA.
AC D6J8W3;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Trimethylamine-N-oxide reductase {ECO:0000256|ARBA:ARBA00011885, ECO:0000256|RuleBase:RU368014};
DE Short=TMAO reductase {ECO:0000256|RuleBase:RU368014};
DE EC=1.7.2.3 {ECO:0000256|ARBA:ARBA00011885, ECO:0000256|RuleBase:RU368014};
GN Name=torA {ECO:0000256|RuleBase:RU368014};
GN ORFNames=ECEG_00310 {ECO:0000313|EMBL:EFF12328.2};
OS Escherichia coli B354.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=550677 {ECO:0000313|EMBL:EFF12328.2, ECO:0000313|Proteomes:UP000004683};
RN [1] {ECO:0000313|EMBL:EFF12328.2, ECO:0000313|Proteomes:UP000004683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B354 {ECO:0000313|EMBL:EFF12328.2,
RC ECO:0000313|Proteomes:UP000004683};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Gordon D.M., Johnson J.R., Johnston B.D., Young S., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Walk T., White J., Yandava C., Haas B., Henn M.R., Nusbaum C., Birren B.;
RT "The Genome Sequence of Escherichia coli B354.";
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an
CC anaerobic reaction coupled to energy-yielding reactions.
CC {ECO:0000256|ARBA:ARBA00003013, ECO:0000256|RuleBase:RU368014}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 Fe(III)-[cytochrome c] + H2O + trimethylamine = 2 Fe(II)-
CC [cytochrome c] + 3 H(+) + trimethylamine N-oxide;
CC Xref=Rhea:RHEA:24236, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15724,
CC ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:58389; EC=1.7.2.3;
CC Evidence={ECO:0000256|ARBA:ARBA00029296,
CC ECO:0000256|RuleBase:RU368014};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|RuleBase:RU368014};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000256|RuleBase:RU368014};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC ECO:0000256|RuleBase:RU368014}.
CC -!- PTM: Exported by the Tat system. {ECO:0000256|RuleBase:RU368014}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312,
CC ECO:0000256|RuleBase:RU368014}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG749328; EFF12328.2; -; Genomic_DNA.
DR RefSeq; WP_001063173.1; NZ_GG749328.1.
DR AlphaFoldDB; D6J8W3; -.
DR Proteomes; UP000004683; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050626; F:trimethylamine-N-oxide reductase (cytochrome c) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009033; F:trimethylamine-N-oxide reductase activity; IEA:UniProtKB-EC.
DR CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR CDD; cd02769; MopB_DMSOR-BSOR-TMAOR; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.90.55.10; Dimethylsulfoxide Reductase, domain 3; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006658; BisC.
DR InterPro; IPR041954; CT_DMSOR/BSOR/TMAOR.
DR InterPro; IPR041460; Molybdopterin_N.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR006311; TAT_signal.
DR InterPro; IPR011887; TorA.
DR NCBIfam; TIGR00509; bisC_fam; 1.
DR NCBIfam; TIGR02164; torA; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR PANTHER; PTHR43742:SF4; TRIMETHYLAMINE-N-OXIDE REDUCTASE 1; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF18364; Molybdopterin_N; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU368014};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505, ECO:0000256|RuleBase:RU368014};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU368014}; Periplasm {ECO:0000256|RuleBase:RU368014};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 55..95
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 99..572
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 690..811
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 848 AA; 94559 MW; 28183B466BFA6D16 CRC64;
MNNNDLFQAS RRRFLAQLGG LTVAGMLGPS LLTPRSATAA QAATEAVTSK EGILTGSHWG
AIRATVKEGR FVAAKPFELD KYPSKMIAGL PDHVHNAARI RYPMVRVDWL RKRHLSDTSQ
RGDNRFVRVS WDEALDMFYE ELERVQKTHG PSALLTASGW QSTGMFHNAS GMLAKAIALH
GNSVGTGGDY STGAAQVILP RVVGSMEVYE QQTSWPLVLQ NSKTIVLWGS DLLKNQQANW
WCPDHDVYEY YEQLKAKVAA GEIEVISIDP VVTSTHEYLG REHVKHIAVN PQTDVPLQLA
LAYTLYSENL YDKNFLANYC VGFEQFLQYL LGEKDGQPKD AAWAEKLTGI DAETIRGLAR
QMAANRTQII AGWCVQRMQH GEQWAWMIVV LAAMLGQIGL PGGGFGFGWH YNGAGTPGRK
GVILSGFSGS SSIPPVHDNS DYKGYSSTIP IARFVDAILE PGKVINWNGK SVKLPPLKMC
IFAGTNPFHR HQQINRIIEG WRKLETVIAI DNQWTSTCRF ADIVLPATTQ FERNDLDQYG
NHSNRGIIAM KQVVPPQFEA RNDFDIFREL CRRFNREEAF TEGLDEMGWL KRIWQEGVQQ
GKGRGVHLPA FDDFWNNKEY VEFDHPQMFV RHQAFREDPD LEPLGTPSGL IEIYSKTIAD
MNYDDCQGHP MWFEKIERSH GGPGSQKYPL HLQSVHPDFR LHSQLCESET LRQQYTVAGK
EPVFINPQDA SARGIRHGDV VRVFNARGQV LAGAVVSDRY APGVARIHEG AWYDPDKGGE
PGALCKYGNP NVLTIDIGTS QLAQATSAHT TLVEIEKYSG TVEQVTAFNG PVEMVAQCEY
VPASQVKS
//
