ID   Q6LS48_PHOPR            Unreviewed;       822 AA.
AC   Q6LS48;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   02-SEP-2026, entry version 123.
DE   RecName: Full=Trimethylamine-N-oxide reductase {ECO:0000256|ARBA:ARBA00069096, 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=STY3956 {ECO:0000313|EMBL:CAG19878.1};
GN   Synonyms=torA {ECO:0000256|RuleBase:RU368014};
GN   OrderedLocusNames=PBPRA1467 {ECO:0000313|EMBL:CAG19878.1};
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=298386 {ECO:0000313|EMBL:CAG19878.1, ECO:0000313|Proteomes:UP000000593};
RN   [1] {ECO:0000313|Proteomes:UP000000593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9 {ECO:0000313|Proteomes:UP000000593};
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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=trimethylamine + 2 Fe(III)-[cytochrome c] + H2O =
CC         trimethylamine N-oxide + 2 Fe(II)-[cytochrome c] + 3 H(+);
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:ARBA00049407,
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   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
CC       {ECO:0000256|PROSITE-ProRule:PRU00648}.
CC   -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC       oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312,
CC       ECO:0000256|RuleBase:RU368014}.
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DR   EMBL; CR378667; CAG19878.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6LS48; -.
DR   STRING; 298386.PBPRA1467; -.
DR   KEGG; ppr:PBPRA1467; -.
DR   eggNOG; COG0243; Bacteria.
DR   HOGENOM; CLU_000422_13_3_6; -.
DR   Proteomes; UP000000593; Chromosome 1.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
DR   GO; GO:0009055; F:electron transfer activity; IEA:TreeGrafter.
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:0009061; P:anaerobic respiration; IEA:TreeGrafter.
DR   CDD; cd02793; MopB_CT_DMSOR-BSOR-TMAOR; 1.
DR   FunFam; 2.40.40.20:FF:000009; Biotin sulfoxide reductase 2; 1.
DR   FunFam; 3.40.228.10:FF:000003; Biotin sulfoxide reductase 2; 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; 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; IPR050612; Prok_Mopterin_Oxidored.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   InterPro; IPR011887; TorA.
DR   NCBIfam; NF011682; PRK15102.1; 1.
DR   NCBIfam; TIGR01409; TAT_signal_seq; 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};
KW   Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|RuleBase:RU368014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000593};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PROSITE-
KW   ProRule:PRU00648}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|RuleBase:RU368014"
FT   CHAIN           36..822
FT                   /note="Trimethylamine-N-oxide reductase"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00648,
FT                   ECO:0000256|RuleBase:RU368014"
FT                   /id="PRO_5029942077"
FT   DOMAIN          45..85
FT                   /note="Molybdopterin oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18364"
FT   DOMAIN          89..562
FT                   /note="Molybdopterin oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF00384"
FT   DOMAIN          678..798
FT                   /note="Molybdopterin dinucleotide-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01568"
SQ   SEQUENCE   822 AA;  92960 MW;  F8E53DB58228F928 CRC64;
     MNMSVSRRSF LKGLATTSAV SVIGPSLLAS SKAMAAETTG TWKTSGSHWG AFRAHVYAGK
     VQEIKPLEMD KYPTDMLNGI KGIIYSPSRV RYPMVRLDWL KKHKYSGETR GNNRFIRMTW
     DDALDLFYRE LERVQKDYGP WALHAGQTGW RQTGQFHSCT SHMQRAVGMH GNFITKVGDY
     STGAGQTILP YVLGSTEVYA QGTSWSEILD HSKNIVLWAT DPVKNLQVGW NCETHESFAY
     LEQLKEKVAK GEINVLSVDP VKNKTQRFLG NDHMYINPQT DVAFMLAVAH TLYTEDLYDK
     EFIKMYCLGF DEFVPYFMGK SKDNIEKTPE WAAEICGLPA DEIRDFARML VAERTQILFG
     WCIQRQEHGE QPYWMGAVIA AMVGQIGLPG GGVSYGHHYS SIGVPSTGFA APGGFPRNVD
     EGQKPKWDNN DFNGYSRTIP VARWVDCLLE PGKEIKYNGS KVILPDYKMM IISGNNPWHH
     HQDRNRMKQA FQKLQTVVTI DFAWTATCRF SDIVLPACTQ FERNDIDVYG SYSGRGLVAM
     HKLVDPLYQS KTDFDIFTEL SRRFGRHKEY TRGMDEMEWV RSLYSDCRDA NKAKFDMPEF
     DEFWAKGVLD FGEGTPWVRH ADFREDPEIN ALGTPSGFIE ISSRKIDRFG YEHCQGHPMW
     FEKSERSHGG PGSKKHPFWM QSCHPDKRLH SQMCESEEMR ATYAVKGREP VYINPKDAAE
     KGIKDGDIVR VFNDRGQLLA GAVLSDSYAR GVIRIEEGAW YGPLNEKVGA IDTYGDPNTL
     TQDIPSSELA QATSANTCLV DFEKFKGEVP PVTSFGGPIE VS
//