ID Q9KQP8_VIBCH Unreviewed; 815 AA.
AC Q9KQP8;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=trimethylamine-N-oxide reductase {ECO:0000256|ARBA:ARBA00011885};
DE EC=1.7.2.3 {ECO:0000256|ARBA:ARBA00011885};
GN OrderedLocusNames=VC_1950 {ECO:0000313|EMBL:AAF95098.1};
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277 {ECO:0000313|EMBL:AAF95098.1, ECO:0000313|Proteomes:UP000000584};
RN [1] {ECO:0000313|EMBL:AAF95098.1, ECO:0000313|Proteomes:UP000000584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961
RC {ECO:0000313|Proteomes:UP000000584};
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D., Ermolaeva M.D.,
RA Vamathevan J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.,
RA Utterback T., Fleishmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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DR EMBL; AE003852; AAF95098.1; -; Genomic_DNA.
DR PIR; H82137; H82137.
DR RefSeq; NP_231584.1; NC_002505.1.
DR RefSeq; WP_000161719.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KQP8; -.
DR STRING; 243277.VC_1950; -.
DR DNASU; 2613454; -.
DR EnsemblBacteria; AAF95098; AAF95098; VC_1950.
DR KEGG; vch:VC_1950; -.
DR PATRIC; fig|243277.26.peg.1864; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0030151; F:molybdenum ion binding; IBA:GO_Central.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0050626; F:trimethylamine-N-oxide reductase (cytochrome c) activity; IEA:UniProtKB-EC.
DR GO; GO:0009033; F:trimethylamine-N-oxide reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR CDD; cd02777; MopB_CT_DMSOR-like; 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; 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 NCBIfam; TIGR00509; bisC_fam; 1.
DR NCBIfam; TIGR01409; TAT_signal_seq; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR PANTHER; PTHR43742:SF10; TRIMETHYLAMINE-N-OXIDE REDUCTASE 2; 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; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000000584};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 42..82
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 86..555
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 675..791
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 815 AA; 89440 MW; 8B1D3DC21BFE8FEA CRC64;
MTKITRRGFL KGTGMAAGAM AFTSFSPLSI ASDNARGKGV LTAGRMGPLL CEVQDGKMVA
TKNALAQTVP NSLQSTGPDQ VYTQARVKYP MVRKGFLANP AAPKGVRGSD EFVRVSWDDA
YRLIHEQHMR IRKTYGPASV FAGSYGWRSS GVLHKAQTLL QRYMSMAGGY SGHLGDYSTG
AAQIIMPHVV GSIEVYEQQT TYPVVLEHSD VVVLWGLNPI NTLKIAWSST DCAGLEFFHQ
LKKSGKTIIG IDPIRSETIE FFGEQAQWIA PHPMTDVAMM MGIAHSLIKQ GKHDKAFLDK
YTVGYDRFEA YLLGKEDGVE KSAQWAEGIC GVPAKQLETL AEIFSNHRTM LMAGWGMQRQ
QYGEQRHWMV VTLAAMLGQI GLPGGGFGFS YHYSNGGNPA RDAGVLPAIS AAIGGGSSAG
NDWAISGATQ SFPVARIVEA LENPGGAYQH NGHTLTFPEI KMIWWAGGAN FTHHQDTNRL
IKAWQKPELI VISEPYWTAA AKHADIVLPI TTTFERNDLT MTGDYSNQHL VPMKQVVEPQ
GEARNDFDVF ADMAEMIRPG GRDVFTEGKT EMEWLYGFYK TAQKSGRAAR VAMPNFSKFW
EDNQLIEMKW NAKNAQFVRY ADFRADPILN PLGTPSGKIE IYSKTLAGFN LPDCPAHPTW
LAPDEFTGNA KQGELQLMTA HAAHRLHSQF NYAQLREEYA IANREPIWIH PEDAASRGIQ
TGDLVRAYNQ RGQVLVGALV TDRIKQGSVC IHEGGWPDLD PQTGLCKNGG ANVLTSDIPT
SRLANGCAAN SSLVRIEKYT GPALELTAFM PPKNG
//
