ID B7LTG1_ESCF3 Unreviewed; 759 AA.
AC B7LTG1;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Biotin sulfoxide reductase {ECO:0000313|EMBL:CAQ91020.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:CAQ91020.1};
GN Name=bisC {ECO:0000313|EMBL:CAQ91020.1};
GN OrderedLocusNames=EFER_3548 {ECO:0000313|EMBL:CAQ91020.1};
OS Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS 14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585054 {ECO:0000313|EMBL:CAQ91020.1, ECO:0000313|Proteomes:UP000000745};
RN [1] {ECO:0000313|Proteomes:UP000000745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 /
RC JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73
RC {ECO:0000313|Proteomes:UP000000745};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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}.
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DR EMBL; CU928158; CAQ91020.1; -; Genomic_DNA.
DR AlphaFoldDB; B7LTG1; -.
DR KEGG; efe:EFER_3548; -.
DR HOGENOM; CLU_000422_13_3_6; -.
DR Proteomes; UP000000745; Chromosome.
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:UniProtKB-KW.
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; 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; 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};
KW Oxidoreductase {ECO:0000313|EMBL:CAQ91020.1}.
FT DOMAIN 38..499
FT /note="Molybdopterin oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF00384"
FT DOMAIN 618..723
FT /note="Molybdopterin dinucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF01568"
SQ SEQUENCE 759 AA; 84056 MW; 538599C64C9DE62D CRC64;
MLVETDGETV FSSRGALARG MDNSLQSAVR DQVHSNTRVR FPMVRKGFLA SPENPQGIRG
QDEFVRVSWD EALDLIHQQH KRIREAYGPA SIFAGSYGWR SNGVLHKAST LLQRYMALAG
GYTGHLGDYS TGAAQAIMPY VVGGSEVYQQ QTSWPLVLEH SDVVVLWSAN PLNTLKIAWN
ASDEQGLSYF SALRDSGKKL ICIDPMRSET VDFFGDKMEW VAPHMGTDVA LMLGIAHTLV
ENGWHDEAFL ARCTTGYDVF SSYLLGESDG IAKTAEWAAE ICGVNAEKIR ELAAIFQQNT
TMLMAGWGMQ RQQFGEQKHW MIVTLAAMLG QIGTPGGGFG LSYHFANGGN PTRRAAVLSS
MQGSLPGGTD AVDKIPVARI VEALENPGGA YQHNGMNRHF PDIRFIWWAG GANFTHHQDT
NRLIRAWQKP ELVVISECFW TAAAKHADIV LPATTSFERN DLTMTGDYSN QHLVPMKQVV
PPRDEARNDF DVFAGLSERW EKGGFARFTE GKSELQWLET FYNVARQRGA SQQVELPPFA
EFWEANQLIE MPEHPDGERF IRFADFRRDP QAHPLKTVSG KIEIFSQRIA DYAYPDCPGH
PMWLEPDEWQ GNAEPEQLQV LSAHPAHRLH SQLNYSSLRE LYAVANREPI TIHPEDALAR
GIKEGDIVRV WNSRGQILAG AVISEGIKPG VICIHEGAWP DLDLTADGIC KNGAVNVLTK
DLPSSRLGNG CAGNTALAWL EKYNGPELPL TAFDPPASS
//
