ID B1R527_CLOPF Unreviewed; 662 AA.
AC B1R527;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=Molybdopterin oxidoreductase {ECO:0000313|EMBL:EDT24726.1};
GN ORFNames=AC1_1947 {ECO:0000313|EMBL:EDT24726.1};
OS Clostridium perfringens B str. ATCC 3626.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=451754 {ECO:0000313|EMBL:EDT24726.1, ECO:0000313|Proteomes:UP000004342};
RN [1] {ECO:0000313|EMBL:EDT24726.1, ECO:0000313|Proteomes:UP000004342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B str. ATCC 3626 {ECO:0000313|Proteomes:UP000004342};
RA Paulsen I., Sebastian Y.;
RT "Annotation of Clostridium perfringens B str. ATCC 3626.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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:EDT24726.1}.
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DR EMBL; ABDV01000004; EDT24726.1; -; Genomic_DNA.
DR RefSeq; WP_003456053.1; NZ_ABDV01000004.1.
DR AlphaFoldDB; B1R527; -.
DR Proteomes; UP000004342; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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; cd02766; MopB_3; 1.
DR CDD; cd02775; MopB_CT; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR Gene3D; 3.30.2070.10; Formate dehydrogenase/DMSO reductase; 1.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR PANTHER; PTHR43742:SF6; OXIDOREDUCTASE YYAE-RELATED; 1.
DR PANTHER; PTHR43742; TRIMETHYLAMINE-N-OXIDE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 1..58
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 662 AA; 75264 MW; A50ACAA50ECEBAB7 CRC64;
MEVLSHGCTL DCFDCCKFNV YKEGSEILKI EGDKEHPFTK GLICKKGVAH LNRLNHKDRI
YTPLLKNNGV WEEISFEDAL EIMKEKLEYT KEKYSSKSIL YYSQYGSGGV LKGIEDIFFN
FYGGVSKATG GPCWSAGMRA QKYDFGDSVS NSLEDMINSK NIFLWGKNPA NTTIHTMAIL
NKAKKNGSRI IVIDPINTQS AKLGDIHVKI KPGTDGALAM AMAKIIISKG LQDKDFINKY
VLGFQEYKDH LENFDLDYLS DECGIEIEDI EKLTKYYCEK NSSIYLGYGM QKYKNGGNTI
RAIDALGALT GQIGVKGGGV NYANKVLSRI LDSDPFKSGE VGENREFYVS NINEFIEEPK
KYSLSVEDSN APIKIMVIAN SNLMNQLPNL NRLNNSIDKV EFKVCFDMFM TDTASKCDLF
IPCTNTLESE DMVFSSMTNP YLIYNEKIIE PREKLMDEYY FFRELAKRMN LKGYPSLSKK
DYLSKVIEPL MRYNKDITLD YLKNNPFTVY DDVAWENKKF KTPSGKFELA SKRALKECGS
LTPTYLSPRI KENCFRLLTN HSKDSLSSQH YIDVDEKAKV YLNENMIRKF SLICGEKVKL
KSRTGEITAI CSLDNGVQDY VALMYVGWWK KHGNPNFLTE SGISDMGGQI TYNETFIEIE
NI
//
