TORA_VIBCH
ID TORA_VIBCH Reviewed; 820 AA.
AC Q9KRF0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
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=VC_1692;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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; AE003852; AAF94842.1; -; Genomic_DNA.
DR PIR; G82168; G82168.
DR RefSeq; NP_231328.1; NC_002505.1.
DR RefSeq; WP_001018812.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KRF0; -.
DR SMR; Q9KRF0; -.
DR STRING; 243277.VC_1692; -.
DR DNASU; 2613823; -.
DR EnsemblBacteria; AAF94842; AAF94842; VC_1692.
DR KEGG; vch:VC_1692; -.
DR PATRIC; fig|243277.26.peg.1619; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR OMA; KPWVRHA; -.
DR BioCyc; VCHO:VC1692-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0030151; F:molybdenum ion binding; IBA:GO_Central.
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 GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
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; Reference proteome;
KW 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_0000019159"
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; 92305 MW; 6C1BF9FE639DBD82 CRC64;
MAITRRSFLK GVATTSAASI IGPSLLTSVS AQAAETTGTW KVSGSHWGAF RAHIYGGKVQ
ELKALELDTH PTEMLNGIQG ILYSPSRVRY PMVRLDWLKK HKYSAETRGN NRFIRVTWDE
AIDLFYRELE RVQKQYGPWA LHAGQTGWNQ TGAFHNCTAM MQRAVGMHGN YITKVGDYST
GAGQTIMPYV LGSTEVYAQG TSWSEILDNS DNIILWANDP VKNLQVGWNC ETHQSFGYLD
QLKEKVAKGE INVVSVDPVK NKTQRFLQND HLYINPQTDV AFMLALAHVL YTENLYDKKF
IETYCLGFEE FIPYVLGKSK DKVEKTPEWA ATICGVKPDA IRDFARMLVN GRTQLLFGWC
IQRQEHGEQP YWMGAVLAAM IGQIGLPGGG ISYGHHYSGI GVPSTGFAGP GGFPRNLDQG
AKPKWDNNDF NGYSRTIPVA RWIDAILEPG KKINHNGNTV TLPGFKMMVI SGCNPWHHHQ
DRNKMKRAFQ KLETVVTIDF SWTATCRFSD IVLPACTQWE RNDIDSYGSY SGKGLIAMHR
LVDPLFQSRT DFEIMTELTR RFGREKEYTR GMDEMEWVRS LYDECKKANE GKFAMPEFEE
FWEKGFLDFG TGTPWVRHAD FRKDPEINAL GTPSGFIEIT SRKIGRYGYE HCQEHPMWFE
KTERSHGGPG SDKHPFWLQS CHPDKRLHSQ MCEAEAFRAT YAVQGREPVY INPLDAKAKG
IKDGDLVRVF NDRGQLLAGA VLSDSYPRGV IRIEEGAWYG PLTEKVGAIC TYGDPNTLTL
DLGTSELAQA TSANTCIVDF EKFRGEVPPV TSFGGPIEVI
