ID Q0T638_SHIF8 Unreviewed; 848 AA.
AC Q0T638;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2006, sequence version 1.
DT 27-MAR-2024, entry version 102.
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 ECO:0000313|EMBL:ABF03227.1};
GN OrderedLocusNames=SFV_1007 {ECO:0000313|EMBL:ABF03227.1};
OS Shigella flexneri serotype 5b (strain 8401).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=373384 {ECO:0000313|EMBL:ABF03227.1, ECO:0000313|Proteomes:UP000000659};
RN [1] {ECO:0000313|EMBL:ABF03227.1, ECO:0000313|Proteomes:UP000000659}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8401 {ECO:0000313|EMBL:ABF03227.1,
RC ECO:0000313|Proteomes:UP000000659};
RX PubMed=16822325; DOI=10.1186/1471-2164-7-173;
RA Nie H., Yang F., Zhang X., Yang J., Chen L., Wang J., Xiong Z., Peng J.,
RA Sun L., Dong J., Xue Y., Xu X., Chen S., Yao Z., Shen Y., Jin Q.;
RT "Complete genome sequence of Shigella flexneri 5b and comparison with
RT Shigella flexneri 2a.";
RL BMC Genomics 7:173-173(2006).
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}.
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DR EMBL; CP000266; ABF03227.1; -; Genomic_DNA.
DR RefSeq; WP_001063113.1; NC_008258.1.
DR AlphaFoldDB; Q0T638; -.
DR KEGG; sfv:SFV_1007; -.
DR HOGENOM; CLU_000422_13_3_6; -.
DR Proteomes; UP000000659; Chromosome.
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 58..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; 94703 MW; 24AC42B5AC10A382 CRC64;
MNNNDLFQAS RRRFLAQLGG LTVAGMLGPS LLTPRRATAA QAATEAVISK EGILTGLHWG
AIRAMVKDGR FVAAKPFELD KYPSKMIAGL PDHVHNAARI RYPMVRVDWL RKRHLSDTSQ
RGDNRFVRVS WDEALDMFYE ELERVQKTHG PSALLTASGW QSTGMFHNAS GMLAKAIALH
GNSVGTGGDY STGAAQVILP RVVGSMEVYE QQTSWPLVLQ NSKTIVLWGS DLLKNQQANW
WCPDHDVYEY YEQLKAKVAA GEIEVISIDP VVTSTHEYLG REHVKHIAVN PQTDVPLQLA
LAHTLYSENL YDKNFLANYC VGFEQFLPYL LGEKDGQPKD AAWAEKLTGI DAETIRGLAR
QMAANRTQII AGWCVQRMQH GEQWAWMIVV LAAMLGQIGL PGGGFGFGWH YNGAGTPGRK
CVILSGFSGS TSIPPVHDNS DYKGYSSTIP IARFIDAILE 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 SARGIRNGDV VRVFNARGQV LAGAVVSDRY APGVARIHEG AWYDPDKGGE
PGALCKYGNP NVLTIDIGTS QLAQATSAHT TLVEIEKYNG TVEQVTAFNG PVEMVAQCEY
VPASQVKS
//
