ID Q65V15_MANSM Unreviewed; 824 AA.
AC Q65V15;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=trimethylamine-N-oxide reductase {ECO:0000256|ARBA:ARBA00011885};
DE EC=1.7.2.3 {ECO:0000256|ARBA:ARBA00011885};
GN Name=bisC {ECO:0000313|EMBL:AAU37195.1};
GN OrderedLocusNames=MS0588 {ECO:0000313|EMBL:AAU37195.1};
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988 {ECO:0000313|EMBL:AAU37195.1, ECO:0000313|Proteomes:UP000000607};
RN [1] {ECO:0000313|EMBL:AAU37195.1, ECO:0000313|Proteomes:UP000000607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E {ECO:0000313|EMBL:AAU37195.1,
RC ECO:0000313|Proteomes:UP000000607};
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
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; AE016827; AAU37195.1; -; Genomic_DNA.
DR RefSeq; WP_011199767.1; NC_006300.1.
DR AlphaFoldDB; Q65V15; -.
DR STRING; 221988.MS0588; -.
DR KEGG; msu:MS0588; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_3_6; -.
DR OrthoDB; 9815647at2; -.
DR Proteomes; UP000000607; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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 NCBIfam; TIGR00509; bisC_fam; 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; PS00932; MOLYBDOPTERIN_PROK_3; 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 Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 52..92
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 96..562
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 680..801
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 824 AA; 91234 MW; 790A835700F3CDBA CRC64;
MKKVNNSRRN FLKSSSLGFA GASMATATTG GITGLLSVTA NAAETNSKTV VTAAHWGPLG
VVVENGKVVK SGPAIAAPIE NELQSVVADQ LYSEARVKYP MVRKGYLDGN QDRSLRGHDT
WVRISWEQAF DLVAKEMKRV RETYGASGIF AGSYGWYSSG ALHAARTLLH RYMNITGGFV
GTKGDYSTGA AQVIMPHVLG TIEVYEQQTS WEVILESSDT IVLWGANPLA TMRIAWTSTD
QKGLEYFKKF KETGKRIICI DPVRSESCEY LGAEWIPINT GTDVPLMLGI AHTLVNENKH
DKEFLKNYTT GYDKFEEYLL GKIDNQPKTA EWAEKICGVP AQTIKQLAAD FSAKRTMLMG
GWGMQRQRHG EQSHWMMVTL ASMLGQIGLP GGGFGLSYHY SNGGVPTARG GILGSITANP
STQAGAKTWL DDVSKFSFPL ARISDALLNP GKTIQYNGTE VTYPDIKLIY WAGGNPFVHH
QDTNTMVKAW QKPETIIVNE VNWTPTARMA DIVLPATTSY ERNDLTMSGD YSMMNIFPMK
QVVEPQFEAK SDYDIFAELA KRAGVEEQFT EGKTEMQWLK GFYETAFNAA RANRVLMPKF
DDFWNENKPI TFNPTDSAKK WVRYAEFRED PLLNPLGTPS GKIEIYSNTI AKMNYDDCKG
YPSWMEPEEF AGNVTAEEPL ALVTPHPYYR LHSQLAHTSL REKYAVKDRE PVLIHKDDAA
ARGIANGDIV RVFNKRGQVL TGAVVTDGVI KGTVAIHEGA WYDPLDLGQT ERPLCKNGCV
NVLTRDEGTS KLAQGNSPNT CIVQVEKYTG EVPEVTVFKQ PKIA
//
