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Database: UniProt
Entry: G5Q9A1_SALMO
LinkDB: G5Q9A1_SALMO
Original site: G5Q9A1_SALMO 
ID   G5Q9A1_SALMO            Unreviewed;       767 AA.
AC   G5Q9A1;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Biotin sulfoxide reductase {ECO:0000313|EMBL:EHC73978.1};
GN   ORFNames=LTSEMON_5008 {ECO:0000313|EMBL:EHC73978.1};
OS   Salmonella enterica subsp. enterica serovar Montevideo str. S5-403.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=913242 {ECO:0000313|EMBL:EHC73978.1, ECO:0000313|Proteomes:UP000003221};
RN   [1] {ECO:0000313|EMBL:EHC73978.1, ECO:0000313|Proteomes:UP000003221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S5-403 {ECO:0000313|EMBL:EHC73978.1,
RC   ECO:0000313|Proteomes:UP000003221};
RX   PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA   den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA   Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA   Furtado M.R., Wiedmann M.;
RT   "Genome sequencing reveals diversification of virulence factor content and
RT   possible host adaptation in distinct subpopulations of Salmonella
RT   enterica.";
RL   BMC Genomics 12:425-425(2011).
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:EHC73978.1}.
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DR   EMBL; AFCS01001130; EHC73978.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5Q9A1; -.
DR   PATRIC; fig|913242.3.peg.4328; -.
DR   Proteomes; UP000003221; 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;  84765 MW;  4312D34360EBC7B5 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 DWKDEAFLAR CTTGYDRFAD YLLGKTDGTA KTAEWAAEIC GVSAVKIREL
     AEIFHHNTTM LMAGWGMQRQ QFGEQKHWMI VTLAAMLGQI GTPGGGFGFS YHFANGGNPT
     RRAAVLASMQ GSIPGGVDAV DKIPVARIVD ALENPGGFYQ HNGMDRRFPD IRFIWWAGGA
     NFTHHQDTNR LIRAWQKPEL VVISECFWTA AAKHADIVLP ATTSYERNDL TMTGDYSNQH
     LAPMKQVVSP RWEARNDFDV FAELSERWEV GGYARFTEGK SELAWLETFY NIAAQRGASQ
     GVTLPPFAAF WQANRLLEMP ENPANAQFVR FADFRRDPDN HPLKTASGKI EIYSARIASY
     GYADCPGHPM WLVPDEWHGN ADAGQVQLLS AHPAHRLHSQ LNYSSLRERY AVAGREPVTI
     HPQDATTRGI VDGDTVRVWN HRGQVLAGAV VTDGIRPGVI CIHEGAWPDP EPTAGGICKN
     GAVNVLTKDL PSSRLGNGCA GNTALVWFEK YTGPALPLTA FDPPANS
//
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