ID A0A099LKH7_9VIBR Unreviewed; 820 AA.
AC A0A099LKH7;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
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 ORFNames=EA26_15690 {ECO:0000313|EMBL:KGK08673.1};
OS Vibrio navarrensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=29495 {ECO:0000313|EMBL:KGK08673.1, ECO:0000313|Proteomes:UP000029994};
RN [1] {ECO:0000313|EMBL:KGK08673.1, ECO:0000313|Proteomes:UP000029994}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51183 {ECO:0000313|EMBL:KGK08673.1,
RC ECO:0000313|Proteomes:UP000029994};
RA Gladney L.M., Katz L.S., Marino-Ramirez L., Jordan I.K.;
RT "Genome sequencing of Vibrio navarrensis strains.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGK08673.1}.
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DR EMBL; JMCG01000002; KGK08673.1; -; Genomic_DNA.
DR RefSeq; WP_039429640.1; NZ_MPKR01000003.1.
DR AlphaFoldDB; A0A099LKH7; -.
DR STRING; 29495.EA26_15690; -.
DR eggNOG; COG0243; Bacteria.
DR Proteomes; UP000029994; Unassembled WGS sequence.
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 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; IPR006311; TAT_signal.
DR InterPro; IPR019546; TAT_signal_bac_arc.
DR InterPro; IPR011887; TorA.
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:UP000029994};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU368014}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|RuleBase:RU368014"
FT CHAIN 34..820
FT /note="Trimethylamine-N-oxide reductase"
FT /evidence="ECO:0000256|RuleBase:RU368014"
FT /id="PRO_5029946785"
FT DOMAIN 43..83
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 87..561
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 676..796
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 820 AA; 92489 MW; 3D6436570649E953 CRC64;
MAITRRSFLK GVATTSAASV IGPSLLASAS AHAVETTGTW KVSGSHWGAF RAHIYAGKVQ
EIKPLELDKN PTEMLNGIKG IIYSPSRVRY PMVRLDWLKK HKYSADTRGN NRFVRVTWDE
ALDLFYRELE RVQKEYGPWA LHAGQTGWNQ TGSFNNCTAH MQRAVGMHGN YITKVGDYST
GAGQTILPYV LGSTEVYAQG TSWSEILENA DNIILWANDP VKNLQVGWNC ETHESFAYLE
QLRDKVAKAE IKVISVDPVK NKTQRYLQNE HLYVNPMTDV PFMLAIAHVL YNENLYDKKF
IETYCLGFVE FIDYVQGKTK DKVAKTPEWA AEICGVQADK IREFARMLVG GRTQILMGWC
IQRQEHGEQP YWAAAVLAAM IGQIGLPGGG ISYGHHYSSI GVPSTGFAGP GGFPRNLDTG
MKPKWDNNDF NGYSRTIPVA RWIDCLLEPG KEINYNGGKV KLPDFKMMVI SGCNPWHHHQ
DRNRMKQAFQ KLQTVVTIDF AWTATCRFSD IVLPACTQWE RNDIDVYGSY SSRGLIAMHR
LVDPLFQSKP DFQIMKELTE RFGRSEEYSR GMSEMDWIRS LYNDCKKANQ GKFEMPEFDE
FWEKSVLDFG QGKPWVRHAD FRQDPEINPL GTPSGFIEIT SRKIGRYGYE HCQEHPMWFE
KSERSHGGPG SDKHPFWLQS CHPDKRLHSQ MCESEAFRAT YAVQGREPVY INPQDAKAKG
IKQGDLVRVF NDRGQLLAGA VLSDSYPRGV IRIEEGAWYG PLSEKLGAMD TYGDPNTLTQ
DIGSSELAQA TSANTCIVDF EKFTGKVPPV TSFGGPIEVA
//
