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Database: UniProt
Entry: C6PV19_9CLOT
LinkDB: C6PV19_9CLOT
Original site: C6PV19_9CLOT 
ID   C6PV19_9CLOT            Unreviewed;       296 AA.
AC   C6PV19;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   SubName: Full=Oxidoreductase FAD/NAD(P)-binding domain protein {ECO:0000313|EMBL:EET86914.1};
GN   ORFNames=CcarbDRAFT_2636 {ECO:0000313|EMBL:EET86914.1};
OS   Clostridium carboxidivorans P7.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536227 {ECO:0000313|EMBL:EET86914.1, ECO:0000313|Proteomes:UP000004198};
RN   [1] {ECO:0000313|EMBL:EET86914.1, ECO:0000313|Proteomes:UP000004198}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P7 {ECO:0000313|EMBL:EET86914.1,
RC   ECO:0000313|Proteomes:UP000004198};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L., Hemme C.L.;
RT   "The draft genome of Clostridium carboxidivorans P7.";
RL   Submitted (JUN-2009) 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};
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:EET86914.1}.
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DR   EMBL; ACVI01000041; EET86914.1; -; Genomic_DNA.
DR   RefSeq; WP_007061521.1; NZ_GG770677.1.
DR   AlphaFoldDB; C6PV19; -.
DR   STRING; 536227.Ccar_18645; -.
DR   KEGG; cck:Ccar_18645; -.
DR   PATRIC; fig|536227.13.peg.3902; -.
DR   eggNOG; COG0543; Bacteria.
DR   OrthoDB; 9778346at2; -.
DR   Proteomes; UP000004198; Unassembled WGS sequence.
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; IPR001433; OxRdtase_FAD/NAD-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   Pfam; PF00175; NAD_binding_1; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004198}.
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         230
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         233
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         245
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
SQ   SEQUENCE   296 AA;  32702 MW;  76AF9D9220B3F5DB CRC64;
     MYKIVDKREL APNIFLMDIE APRVAKSAKP GQFVIIKMDE KGERIPLTIC DYDAQKGTVT
     IVFQTLGGST QKMADYEIGQ TFRDFVGPLG QPTDLANESI GELKKKNIIF VAGGVGAAPV
     YPQVKWLHQH GIDADVIVGC KSKEYLLLEE EMKSVSGNLY IATDNGTYGY KGFVTDLLTE
     LIEKEGKKYD HVVAIGPMIM MKFICKVTKG FGIKTIVSLN PIMVDGTGMC GACRVTVGGE
     TKFACVDGPE FDGHLVDFEE AMRRQRLYKT EEGKSLMEEQ ERKEGHVCHV GLDGDK
//
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