ID O67867_AQUAE Unreviewed; 279 AA.
AC O67867;
DT 01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT 01-AUG-1998, sequence version 1.
DT 02-APR-2025, entry version 108.
DE RecName: Full=Dihydroorotate dehydrogenase electron transfer subunit iron-sulphur cluster binding domain-containing protein {ECO:0000259|Pfam:PF10418};
GN OrderedLocusNames=aq_2098 {ECO:0000313|EMBL:AAC07835.1};
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Pseudomonadati; Aquificota; Aquificia; Aquificales; Aquificaceae;
OC Aquifex.
OX NCBI_TaxID=224324 {ECO:0000313|EMBL:AAC07835.1, ECO:0000313|Proteomes:UP000000798};
RN [1] {ECO:0000313|EMBL:AAC07835.1, ECO:0000313|Proteomes:UP000000798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5 {ECO:0000313|EMBL:AAC07835.1,
RC ECO:0000313|Proteomes:UP000000798};
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olson G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE000657; AAC07835.1; -; Genomic_DNA.
DR PIR; G70479; G70479.
DR RefSeq; NP_214436.1; NC_000918.1.
DR RefSeq; WP_010881372.1; NC_000918.1.
DR AlphaFoldDB; O67867; -.
DR STRING; 224324.aq_2098; -.
DR EnsemblBacteria; AAC07835; AAC07835; aq_2098.
DR KEGG; aae:aq_2098; -.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_003827_1_0_0; -.
DR InParanoid; O67867; -.
DR OrthoDB; 9778346at2; -.
DR Proteomes; UP000000798; 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: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; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR050353; PyrK_electron_transfer.
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.
PE 4: Predicted;
KW 2Fe-2S {ECO:0000256|PIRSR:PIRSR006816-2};
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:UP000000798}.
FT DOMAIN 209..245
FT /note="Dihydroorotate dehydrogenase electron transfer
FT subunit iron-sulphur cluster binding"
FT /evidence="ECO:0000259|Pfam:PF10418"
FT BINDING 218
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000256|PIRSR:PIRSR006816-2"
FT BINDING 221
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"
SQ SEQUENCE 279 AA; 31578 MW; 859A6A44B318BD81 CRC64;
MYKVLRKERL TPKAVLLEVQ DERAKLVKPG QYALVQANEE SEPIPLSFLD VKESSYTFLV
EVGGRATLEI AELVEEKIQF IEAPCGSPFP VKNYGKVLLI SKNWGVAPLI NIGRALKEES
NEIYFVHVAE DEERVFLTKE ASEISEEFLL FTEDGSLGEE GNSEWALGYF IENFGKPDLI
VSAGSNLDSQ MINRFAEERN IPHIAMVNAH ILDANGLCLA CRVLVEGQEK LACIDGPWFD
ASKVDWDYAI QKEAFYKEEE EKALKTFLRE LQRLKARGR
//
