ID V7IKI9_SALET Unreviewed; 767 AA.
AC V7IKI9;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Molybdopterin guanine dinucleotide-containing S/N-oxide reductase {ECO:0000313|EMBL:ETA86438.1};
GN ORFNames=A628_03559 {ECO:0000313|EMBL:ETA86438.1};
OS Salmonella enterica subsp. enterica serovar Cubana str. 76814.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=1192560 {ECO:0000313|EMBL:ETA86438.1, ECO:0000313|Proteomes:UP000018534};
RN [1] {ECO:0000313|EMBL:ETA86438.1, ECO:0000313|Proteomes:UP000018534}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=76814 {ECO:0000313|EMBL:ETA86438.1};
RX PubMed=24459266;
RA Benahmed F.H., Gopinath G.R., Wang H., Jean-Gilles Beaubrun J., Grim C.,
RA Cheng C.M., McClelland M., Ayers S., Abbott J., Desai P., Frye J.G.,
RA Weinstock G., Hammack T.S., Hanes D.E., Rasmussen M.A., Davidson M.K.;
RT "Whole-Genome Sequencing of Salmonella enterica subsp. enterica Serovar
RT Cubana Strains Isolated from Agricultural Sources.";
RL Genome Announc. 2:e01184-13(2014).
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
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:ETA86438.1}.
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DR EMBL; AZGR01000076; ETA86438.1; -; Genomic_DNA.
DR AlphaFoldDB; V7IKI9; -.
DR PATRIC; fig|1192560.4.peg.3338; -.
DR HOGENOM; CLU_000422_13_3_6; -.
DR Proteomes; UP000018534; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
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 NCBIfam; TIGR00509; bisC_fam; 1.
DR PANTHER; PTHR43742:SF5; BIOTIN SULFOXIDE REDUCTASE; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 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.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 2..42
FT /note="Molybdopterin oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF18364"
FT DOMAIN 46..507
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 627..731
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 767 AA; 84718 MW; 7F958CA73ABC793D CRC64;
MTAAHWGPVR VETDGERIFA SYGELPTAHQ NSLQTVVHDQ VHSKTRVRFP MVRKGFLASP
DKPQGIRGQD EFVRVSWDDA LDLIHAQHKR IRESYGPSSI FAGSYGWRSN GVLHKAATLL
QRYMALAGGY TGHLGDYSTG AAQAIMPYVV GGNEVYQQQT SWPVVLEHSE VVVLWSANPL
NTLKIAWNAS DEQGLDYFAA LRQSGKRLIC IDPMRSESVD FFGDKMEWIA PHMGTDVALM
LGIAHTLVEN GWQDEAFLAR CTTGYDRFAD YLLGTTDGTA KTAEWAAEIC GVSAVKIREL
AEIFHHHTTM LMAGWGMQRQ QFGEQKHWMI VTLAAMLGQI GTPGGGFGFS YHFANGGNPT
RRAAVLASMQ GSIPGGVDAV DKIPVARIVE ALENPGGFYQ HNGMDRRFPD IRFIWWAGGA
NFTHHQDTNR LIRAWQKPEL VVISECFWTA AAKHADIVLP ATTSYERNDL TMTGDYSNQH
LAPMKQVVSP RWEARNDFDV FAELSERWEA GGYARFTEGK SELAWLETFY NIAAQRGASQ
GVTLPPFAAF WQANRLLEMP ENPANAQFVR FADFRRDPDN HPLKTASGKI EIYSTRIASY
GYADCPGHPM WLVPDEWHGN ADAGQVQLLS AHPAHRLHSQ LNYSSLRERY AVAGREPVTI
HPQDATTRGI VDGDTVRVWN HRGQVLAGAV VTDGIRPGVI CIHEGAWPDP EPTAGGICKN
GAVNVLTKDL PSSRLGNGCA GNTALVWFEK YTGPALPLTA FDPPANS
//
