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Database: UniProt
Entry: A7GDX1_CLOBL
LinkDB: A7GDX1_CLOBL
Original site: A7GDX1_CLOBL 
ID   A7GDX1_CLOBL            Unreviewed;       295 AA.
AC   A7GDX1;
DT   11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT   11-SEP-2007, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Oxidoreductase, NAD/FAD-binding {ECO:0000313|EMBL:ABS39711.1};
GN   OrderedLocusNames=CLI_1721 {ECO:0000313|EMBL:ABS39711.1};
OS   Clostridium botulinum (strain Langeland / NCTC 10281 / Type F).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441772 {ECO:0000313|EMBL:ABS39711.1, ECO:0000313|Proteomes:UP000002410};
RN   [1] {ECO:0000313|Proteomes:UP000002410}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Langeland / NCTC 10281 / Type F
RC   {ECO:0000313|Proteomes:UP000002410};
RA   Brinkac L.M., Daugherty S., Dodson R.J., Madupu R., Brown J.L., Bruce D.,
RA   Detter C., Munk C., Smith L.A., Smith T.J., White O., Brettin T.S.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR006816-1};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR006816-1};
CC   -!- COFACTOR:
CC       Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC         Evidence={ECO:0000256|PIRSR:PIRSR006816-2};
CC       Note=Binds 1 [2Fe-2S] cluster per subunit.
CC       {ECO:0000256|PIRSR:PIRSR006816-2};
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DR   EMBL; CP000728; ABS39711.1; -; Genomic_DNA.
DR   RefSeq; WP_012099730.1; NC_009699.1.
DR   AlphaFoldDB; A7GDX1; -.
DR   KEGG; cbf:CLI_1721; -.
DR   HOGENOM; CLU_003827_1_0_9; -.
DR   Proteomes; UP000002410; Chromosome.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro.
DR   CDD; cd06219; DHOD_e_trans_like1; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR012165; Cyt_c3_hydrogenase_gsu.
DR   InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR43513; DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER SUBUNIT; 1.
DR   PANTHER; PTHR43513:SF3; DIHYDROOROTATE DEHYDROGENASE B (NAD(+)), ELECTRON TRANSFER SUBUNIT-RELATED; 1.
DR   Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR   PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   2Fe-2S {ECO:0000256|PIRSR:PIRSR006816-2};
KW   FAD {ECO:0000256|PIRSR:PIRSR006816-1};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR006816-1};
KW   Iron {ECO:0000256|PIRSR:PIRSR006816-2};
KW   Iron-sulfur {ECO:0000256|PIRSR:PIRSR006816-2};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR006816-2}.
FT   DOMAIN          1..95
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         62..64
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-1"
FT   BINDING         229
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         232
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         244
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
SQ   SEQUENCE   295 AA;  32685 MW;  C7074D40C85787D4 CRC64;
     MYKIIEKKEL APKIYSIEIE AKRVAKSAKP GQFIIVRIDE KGERIPLTVA DYNKEKGTVT
     IVVQAVGSST NRMVQLEVGD YFMDFVGPLG KPSEFVEEDL ESLKNMKLIF VAGGVGAAPV
     YPQVKWLCER GIKPEVIIGG KSKEFILLEK EMIDLGAKVY PCTDDGSYGF HGLVTNKLKE
     LIDGGENYDR VITIGPMIMM YFVTKLTKEY KLPTIASLNT LMVDGTGMCG ACRVTVGGET
     KFTCVDGPEF DAHLVDFDEA MKRQALYKTE EGKRLHKVEE EKEGHVCHIG AGENA
//
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