ID A0A1Q9HE43_9VIBR Unreviewed; 820 AA.
AC A0A1Q9HE43;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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:KAB1454839.1};
GN ORFNames=BIY22_07420 {ECO:0000313|EMBL:OLQ87997.1}, F7O85_18480
GN {ECO:0000313|EMBL:KAB1454839.1};
OS Vibrio panuliri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1381081 {ECO:0000313|EMBL:OLQ87997.1, ECO:0000313|Proteomes:UP000186313};
RN [1] {ECO:0000313|EMBL:OLQ87997.1, ECO:0000313|Proteomes:UP000186313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 703 {ECO:0000313|EMBL:OLQ87997.1,
RC ECO:0000313|Proteomes:UP000186313};
RA Gonzalez-Castillo A., Gomez-Gil B., Enciso-Ibarra K.;
RT "Genomic Taxonomy of the Vibrionaceae.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAB1454839.1, ECO:0000313|Proteomes:UP000446972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LBS 2 {ECO:0000313|EMBL:KAB1454839.1,
RC ECO:0000313|Proteomes:UP000446972};
RA Das S.S.;
RT "Whole genome sequence of Vibrio panuliri LBS 2.";
RL Submitted (SEP-2019) 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:OLQ87997.1}.
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; WAHU01000009; KAB1454839.1; -; Genomic_DNA.
DR EMBL; MJMJ01000023; OLQ87997.1; -; Genomic_DNA.
DR RefSeq; WP_075709169.1; NZ_WAHU01000009.1.
DR AlphaFoldDB; A0A1Q9HE43; -.
DR STRING; 1381081.BIY22_07420; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000186313; Unassembled WGS sequence.
DR Proteomes; UP000446972; 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 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_5033823147"
FT DOMAIN 43..83
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 87..560
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; 92562 MW; AB6E091503F9C2EE CRC64;
MAITRRSFLK GVATTSAATV IGPSLLASAS ASAAETTGTW KVTGSHWGAF RAHIYAGKVQ
EIKPLELDKN PTEMLNGIKG IIYSPSRVRY PMVRLDWLKK HKYSAETRGN NRFIRVTWDE
ALDLFYRELE RVQKDYGPWA LHAGQTGWNQ TGAFNNCTAH MQRAVGMHGN FITKVGDYST
GAGQTIMPYV LGSTEVYAQG TSWSEILENS DNIVLWANDP VKNLQVGWNC ETHESFKYLA
QLKEKVAKGE INVLSVDPVK NKTQRYLEND HLYINPMTDV AFMLAVAHTL YNENLYDKKF
IETYCLGFED FIGYVQGETK DKVVKTPEWA EEICGVKADK IREFARMLVN GRTQILMGWC
IQRQEHGEQP YWAAAVVAAM VGQIGLPGGG ISYGHHYSSI GVPSTGFAGP GGFPRNLDQG
MKPKWDNNDF NGYSRTIPVA RWIDCLLEPG KEIRYNGGKV KLPDFKMMVI SGCNPWHHHQ
DRNRMKKAFK KLQTVVTVEF AWTATCRFSD IVLPACTQWE RNDIDVYGSY SNKGLVAMHR
LVDPLFQSKP DFQIMSELTQ RFGRRDEYTR GMSEMEWIES LYNDCKAANK GKFEMPEFAE
FWKESVLDFG EGKPWVRHAD FRQDPEINPL GTPSGFIEIT SRKIGRYGYE HCQEHPMWFE
KTERSHGGPG SDKHPFWLQS CHPDKRLHSQ MCESEEFRAT YAVQGREPVY INPLDAKEKG
IKDGDLVRVF NDRGQLMAGA VLTDSYPRGV IRIEEGAWYG PLNEKEGAIC TYGDPNTLTL
DIGSSELAQA TSANTCIVDF EKFKGKVPPV TSFGGPIEVA
//
