ID   TORA_PASMU              Reviewed;         823 AA.
AC   Q9CK41;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=PM1793;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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}.
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; AE004439; AAK03877.1; -; Genomic_DNA.
DR   RefSeq; WP_010907339.1; NC_002663.1.
DR   AlphaFoldDB; Q9CK41; -.
DR   SMR; Q9CK41; -.
DR   STRING; 747.DR93_143; -.
DR   PRIDE; Q9CK41; -.
DR   EnsemblBacteria; AAK03877; AAK03877; PM1793.
DR   KEGG; pmu:PM1793; -.
DR   PATRIC; fig|272843.6.peg.1817; -.
DR   HOGENOM; CLU_000422_13_3_6; -.
DR   OMA; KPWVRHA; -.
DR   Proteomes; UP000000809; Chromosome.
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; 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   Pfam; PF00384; Molybdopterin; 1.
DR   Pfam; PF18364; Molybdopterin_N; 1.
DR   Pfam; PF01568; Molydop_binding; 1.
DR   SUPFAM; SSF50692; SSF50692; 1.
DR   TIGRFAMs; TIGR00509; bisC_fam; 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..32
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           33..823
FT                   /note="Trimethylamine-N-oxide reductase"
FT                   /id="PRO_0000019154"
FT   BINDING         181
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   823 AA;  93357 MW;  BECAC53FABEE250F CRC64;
     MKQSRRQFLK NMSAMAATFA MPNFLIAQNA FAQSAENVSE WKITGSHWGA IRAKVQNGKV
     VDVKPFEYDQ YPTEMIKGIK DLIYSEARIR YPMVRLDWLK KRHNSNTAQR GDNRFVRVTW
     DEALDLFYEE LERIQQNYGP WALHTGNVGW RSTGQFHSCG NHMIRAVGMH GNSVSTSGDY
     STGAGQVILP YVLGSTEVYS QGTSWEIILK ESENIIFWAS DPVKNLQVGW NCETHEAYKY
     LEQLKAKVAA KDVNVICVDP VKSKTQNYLG CDFQYINPQT DVAFMLALAH TLYVENLYDK
     KFIEMYTVGF EKFLPYLLGE SEDKVVKDAE WAAKICAIQA EDIRQFARML AGKRTQLIFG
     WAIQRQQHGE QPYWMGTVLA AMLGQIGLAG GGISYAHHYS SIGIPSSGAA MPGAFPLNLD
     EGQKPKYDNK NYNGYSAVIP CARITDSLLQ PGETIDHNGQ KITYAPYKMA IFTGCNHWHR
     HSERNKMKQA FQRLETIVSI NYSWTATCRF SDIVLPACTP FERNDIDAYG SYSNRGVIAM
     QKLVDPLYDS RSDFEIFKDL CRRFGKEKEY CRNMDEMEWV KHLYEACRQE NQGKFDMPPF
     AEFWQKGYVL FPEGEPWVRH ADFREDPELH ALGTPSGFIE IFSNKIASYG YADCKGHPMW
     FEKAERSHGG PKSDKYPFWL QSAHPDKRLH SQLCESKALR ETYAIQDREP LFINPEDAKR
     LGIVHGDLVR VYNDRGQAIV GAHVSDNFPQ GVLRLQEGAW YSPLDEKVGS IDTYGDPNTM
     SLDIGSSSLA QAVSANTCLV NIEKFVGQAP AVTGFHGPHE VAL