ID   A0A1I4HEK0_9PORP        Unreviewed;       255 AA.
AC   A0A1I4HEK0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Dihydroorotate dehydrogenase electron transfer subunit {ECO:0000313|EMBL:SFL39941.1};
GN   ORFNames=SAMN05216357_12161 {ECO:0000313|EMBL:SFL39941.1};
OS   Porphyromonadaceae bacterium KH3CP3RA.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae.
OX   NCBI_TaxID=1855396 {ECO:0000313|EMBL:SFL39941.1, ECO:0000313|Proteomes:UP000198708};
RN   [1] {ECO:0000313|EMBL:SFL39941.1, ECO:0000313|Proteomes:UP000198708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KH3CP3RA {ECO:0000313|EMBL:SFL39941.1,
RC   ECO:0000313|Proteomes:UP000198708};
RA   de Groot N.N.;
RL   Submitted (OCT-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|ARBA:ARBA00034078};
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   -!- SIMILARITY: Belongs to the PyrK family.
CC       {ECO:0000256|ARBA:ARBA00006422}.
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DR   EMBL; FOSU01000021; SFL39941.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4HEK0; -.
DR   Proteomes; UP000198708; 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; cd06218; DHOD_e_trans; 1.
DR   Gene3D; 2.10.240.10; Dihydroorotate dehydrogenase, electron transfer subunit; 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; IPR037117; Dihydroorotate_DH_ele_sf.
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   PRINTS; PR00409; PHDIOXRDTASE.
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   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|PIRSR:PIRSR006816-2};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   FAD {ECO:0000256|PIRSR:PIRSR006816-1};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR006816-1};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR006816-2};
KW   Iron-sulfur {ECO:0000256|PIRSR:PIRSR006816-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR006816-2};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          1..104
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   BINDING         54..57
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-1"
FT   BINDING         71..73
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-1"
FT   BINDING         78..79
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         227
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         230
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT   BINDING         242
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
SQ   SEQUENCE   255 AA;  28495 MW;  869FA28B668E2B85 CRC64;
     MQVLDFTVRS NEALNDQNHL IKVAPSGNEI LPEMQPGQFV QILVDNSPHV FLRRPISINF
     VDKEKNEIWL LIQKIGEGTE KICSINEGEI MNLIYPLGNS FTLPERNGKY LLIGGGVGTA
     PMLFLGKKMK ESGIEPEFLL GGRSAKDILQ RTDFERYGTL YCTTEDGSFG EKGFVTHHSV
     LKEKKYDFIY TCGPKPMMVA VAKYAHEHGI ECEASLENLM ACGFGACLCC VEKTVRGNIC
     TCTEGPVFNI KELFW
//