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
//