TORA_VIBVU
ID TORA_VIBVU Reviewed; 820 AA.
AC Q8D8S3;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Trimethylamine-N-oxide reductase;
DE Short=TMAO reductase;
DE Short=Trimethylamine oxidase;
DE EC=1.7.2.3;
DE Flags: Precursor;
GN Name=torA; OrderedLocusNames=VV1_2895;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an
CC anaerobic reaction coupled to energy-yielding reactions. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250};
CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-
CC bis-MGD) cofactor per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has not been experimentally proven.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
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DR EMBL; AE016795; AAO11229.2; -; Genomic_DNA.
DR RefSeq; WP_011080716.1; NC_004459.3.
DR AlphaFoldDB; Q8D8S3; -.
DR SMR; Q8D8S3; -.
DR EnsemblBacteria; AAO11229; AAO11229; VV1_2895.
DR KEGG; vvu:VV1_2895; -.
DR HOGENOM; CLU_000422_13_3_6; -.
DR OMA; KPWVRHA; -.
DR Proteomes; UP000002275; Chromosome 1.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0050626; F:trimethylamine-N-oxide reductase (cytochrome c) activity; IEA:UniProtKB-EC.
DR CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
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; IPR019546; TAT_signal_bac_arc.
DR InterPro; IPR011887; TorA.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF18364; Molybdopterin_N; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR TIGRFAMs; TIGR02164; torA; 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; Molybdenum; Oxidoreductase; Periplasm; Signal.
FT SIGNAL 1..33
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 34..820
FT /note="Trimethylamine-N-oxide reductase"
FT /id="PRO_0000019161"
FT BINDING 179
FT /ligand="Mo-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60539"
FT /ligand_part="Mo"
FT /ligand_part_id="ChEBI:CHEBI:28685"
FT /evidence="ECO:0000250"
SQ SEQUENCE 820 AA; 92508 MW; 76231D866025E90C CRC64;
MAITRRSFLK GVATTSAASV IGPSLLASAS ANAVETTGTW KVSGSHWGAF RAHIYAGKVQ
EIKPIELDQN PTEMLNGIKG IIYSPSRVRY PMVRLDWLKK HKYSADTRGN NRFVRVTWDE
ALDLFYRELE RVQKEYGPWA LHAGQTGWNQ TGSFNNCTAH MQRAVGMHGN YITKVGDYST
GAGQTILPYV LGSTEVYAQG TSWSEILENA DNIILWANDP VKNLQVGWNC ETHESYAYLA
QLKEKVAKGE INVISVDPVK NKTQRYLEND HLYVNPMTDV PFMLAIAHVL YTENLYDKKF
IETYCLGFEE FINYVQGKTK DKVEKTPEWA APICGVKADK IREFARMLVK GRTQILMGWC
IQRQEHGEQP YWAAAVVAAM IGQIGLPGGG ISYGHHYSSI GVPSTGFAGP GGFPRNLDAG
MKPKWDNNDF NGYSRTIPVA RWIDCLLEPG KEINYNGGKV KLPDFKMMVI SGCNPWHHHQ
DRNRMKQAFQ KLQTVVTIDF AWTATCRFSD IVLPACTQWE RNDIDVYGSY SSRGLIAMHR
LVDPLFQSKP DFQIMKELTE RFGRSEEYSR GMSEMDWIRS LYNDCKKSNE GKFEMPEFDE
FWEKSVLDFG QGQPWVRHAD FRQDPEINPL GTPSGFIEIT SRKIGRYGYE HCQEHPMWFE
KSERSHGGPG SDKHPFWLQS CHPDKRLHSQ MCESEEFRAT YAVKGREPVY INPLDAKAKG
IKEGDLVRVF NDRGQLLAGA VLTDSYPRGV IRIEEGAWYG PLNEKVGAID TYGDPNTLTQ
DIGSSELAQA TSANTCIVDF EKFTGKVPPV TSFGGPIEVA