ID   M1Z9H1_9FIRM            Unreviewed;       294 AA.
AC   M1Z9H1;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN   ORFNames=CUESP1_0555 {ECO:0000313|EMBL:SHD75940.1};
OS   [Clostridium] ultunense Esp.
OC   Bacteria; Bacillota; Tissierellia; Tissierellales; Tepidimicrobiaceae;
OC   Schnuerera.
OX   NCBI_TaxID=1288971 {ECO:0000313|EMBL:SHD75940.1, ECO:0000313|Proteomes:UP000245423};
RN   [1] {ECO:0000313|EMBL:SHD75940.1, ECO:0000313|Proteomes:UP000245423}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Clostridium ultunense strain Esp {ECO:0000313|EMBL:SHD75940.1};
RA   Manzoor S.;
RL   Submitted (NOV-2016) 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; LT669839; SHD75940.1; -; Genomic_DNA.
DR   RefSeq; WP_005584072.1; NZ_LT669839.1.
DR   AlphaFoldDB; M1Z9H1; -.
DR   HOGENOM; CLU_003827_1_0_9; -.
DR   OrthoDB; 9778346at2; -.
DR   Proteomes; UP000245423; Chromosome chri.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245423}.
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   294 AA;  32027 MW;  4961721ABE9E8520 CRC64;
     MYKIVEKKDL APNIVSMDIL APRVANSAQP GQFIIVIVDE AGERIPLTIC NYDKEKGTVN
     IVIQAMGSST KRIAALNEGD YLKDFVGPLG KPSDYVNADI EEIKKQKVLF VAGGVGAAPV
     FPQVRWFHER GIDVDVIVGA KTKDLVILED EIREVAGNLY IATDDGSYGF NGMVTGLIEE
     LVVNQGKEYD LVISIGPMIM MKFVSLLTKK LGIKTVVSLN PIMVDGTGMC GACRVTVGNE
     TKFACVDGPE FDGHLVDFDE ALKRQAQYKE EEVELAKRGE EKTCTCQHGG VHNG
//