ID N6XAN7_9RHOO Unreviewed; 839 AA.
AC N6XAN7;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 44.
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=C664_06208 {ECO:0000313|EMBL:ENO78791.1};
OS Thauera sp. 63.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=497321 {ECO:0000313|EMBL:ENO78791.1, ECO:0000313|Proteomes:UP000013007};
RN [1] {ECO:0000313|EMBL:ENO78791.1, ECO:0000313|Proteomes:UP000013007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=63 {ECO:0000313|EMBL:ENO78791.1,
RC ECO:0000313|Proteomes:UP000013007};
RA Liu B., Shapleigh J.P., Frostegard A.H.;
RT "Draft Genome Sequences of 6 Strains from Genus Thauera.";
RL Submitted (SEP-2012) 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:ENO78791.1}.
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; AMXC01000005; ENO78791.1; -; Genomic_DNA.
DR RefSeq; WP_004255544.1; NZ_AMXC01000005.1.
DR AlphaFoldDB; N6XAN7; -.
DR eggNOG; COG0243; Bacteria.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000013007; 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; IPR011887; TorA.
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 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00022485};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
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, ECO:0000256|RuleBase:RU368014}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|RuleBase:RU368014"
FT CHAIN 34..839
FT /note="Trimethylamine-N-oxide reductase"
FT /evidence="ECO:0000256|RuleBase:RU368014"
FT /id="PRO_5029941162"
FT DOMAIN 50..90
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 94..568
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 686..806
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 839 AA; 93705 MW; E1A12EF1C2BC38C5 CRC64;
MNYSRRGFLK AMAAMSGSAL VAPGLLTAAP AFAAGEATAV SDDITTWKIS GSHFGAIRAK
VVGDRVVDIR PFEHDKHPTE MIKGLLGLIY SPSRVRYPMV RLDWYRKRHL SDTSQRGDNR
FVRVSWDEAL DLFYEELERI QKDYGPWALH TAGVGWRSVG QVHSCGNHMV RGIGMHGRSV
GTIGDYSTGA GQMILPYVLG STEVYSQGTS WDVILQESKL VVFWANDPIK NLQVGWNTET
HESYAYFEQL KAKVADKSIQ VICIDPVKSK TLNYLGAAEH QYINPMTDVP LMLAIAHTLV
KEGLHDQKFL DTYTLGFDKF LPYLEGKTED QAEKTPEWAE KICGVPADRI RELARLMAKH
RTQLIFGWAV QRQQHGEQPY WMGAVLAAML GQIGLPGGGI SYAHHYSSVG VSSSGAAMPG
AFPLNLDPGR KPKHDNTDYK GYSAVVPIAR VIDALLEPGK EIDFNGGKVK LPPYKMAIFS
GCNQWHRQPQ RNRMKEAWRK LETVVAIDYN WTATCRFADI VLPACTPFER NDLDGYGSYS
NRGIIAMQKL VDPLFHSRTD FEIFRGLTRR FNRDAEYTRG MDEMQWVEKI YEDCRKENGL
KDIAMPPFAE FWKQGYVLFP EGKPWVRHAD FRDDAEVNAL GTPSGFIEIF SRKIDRYGYA
DCKGHPVWME KTERSHGGPG SDRFPLWLQS VHPDKRLHSQ LCESEPLRGT YTIAGREPVF
LGPEDAAARG IKHGDLVRVF NDRGQLLAGA HVSNNFPRGV VRIQEGAWYG PTGPEIGALD
TYGDPNTLTL DIGTSSLAQA TSANTCLVQI EKFVGTPPKV TSFGGPIEVD PEGREVKPA
//
