ID A0A367GFU0_9FIRM Unreviewed; 280 AA.
AC A0A367GFU0;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Sulfide/dihydroorotate dehydrogenase-like FAD/NAD-binding protein {ECO:0000313|EMBL:RCH50942.1};
GN ORFNames=C4885_09070 {ECO:0000313|EMBL:RCH50942.1};
OS Subdoligranulum sp. APC924/74.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Subdoligranulum.
OX NCBI_TaxID=2086273 {ECO:0000313|EMBL:RCH50942.1, ECO:0000313|Proteomes:UP000253465};
RN [1] {ECO:0000313|EMBL:RCH50942.1, ECO:0000313|Proteomes:UP000253465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APC924/74 {ECO:0000313|EMBL:RCH50942.1,
RC ECO:0000313|Proteomes:UP000253465};
RA Fitzgerald B.C., Shkoporov A.N., Ross P.R., Hill C.;
RT "Complete genome sequencing of Faecalibacterium prausnitzii strains
RT isolated from the human gut.";
RL Submitted (FEB-2018) 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:RCH50942.1}.
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DR EMBL; PSQF01000032; RCH50942.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367GFU0; -.
DR OrthoDB; 9778346at2; -.
DR Proteomes; UP000253465; 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; 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:UP000253465}.
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 69..70
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-1"
FT BINDING 222
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 225
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 237
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
SQ SEQUENCE 280 AA; 30345 MW; D86B116D29D3D158 CRC64;
MFKIVKKREL NPTVTEMVIE APLIAKKAKA GQFIIIRAKE DSERIPLTIA HYDAAAGTVA
IIFQIVGAGT MQLNSLKEGE YVHDFVGPLG KATEIEGLKN VCVVGGGVGC AIALPVAQAL
KAQGTKVTGI IGFRNKDLVI LEDEFRACCD ELIIMSDDGS YGQKGVVTMP LEEKIKDGAD
FDEVITIGPL IMMKFVVKTT KPYNVKTVVS MNPIMVDGTG MCGGCRLTVG GKTKFACVDG
PDFDGFEVDF DEAMHRGTMY RDFEAHAREA ECNLLKKEVE
//
