PYRKH_AQUAE
ID PYRKH_AQUAE Reviewed; 251 AA.
AC O67329;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit homolog;
DE AltName: Full=Dihydroorotate oxidase B, electron transfer subunit homolog;
GN OrderedLocusNames=aq_1305;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
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., Olsen 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; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the PyrK family. {ECO:0000305}.
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DR EMBL; AE000657; AAC07287.1; -; Genomic_DNA.
DR PIR; F70412; F70412.
DR RefSeq; NP_213893.1; NC_000918.1.
DR RefSeq; WP_010880831.1; NC_000918.1.
DR AlphaFoldDB; O67329; -.
DR SMR; O67329; -.
DR STRING; 224324.aq_1305; -.
DR EnsemblBacteria; AAC07287; AAC07287; aq_1305.
DR KEGG; aae:aq_1305; -.
DR PATRIC; fig|224324.8.peg.1017; -.
DR eggNOG; COG0543; Bacteria.
DR HOGENOM; CLU_003827_1_2_0; -.
DR InParanoid; O67329; -.
DR OMA; RYMKCGI; -.
DR OrthoDB; 1885467at2; -.
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:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:InterPro.
DR Gene3D; 2.10.240.10; -; 1.
DR Gene3D; 3.40.50.80; -; 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; IPR017938; Riboflavin_synthase-like_b-brl.
DR Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR PIRSF; PIRSF006816; Cyc3_hyd_g; 1.
DR SUPFAM; SSF52343; SSF52343; 1.
DR SUPFAM; SSF63380; SSF63380; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW 2Fe-2S; Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur;
KW Metal-binding; Reference proteome; Transport.
FT CHAIN 1..251
FT /note="Dihydroorotate dehydrogenase B (NAD(+)), electron
FT transfer subunit homolog"
FT /id="PRO_0000148371"
FT DOMAIN 2..101
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00716"
FT BINDING 217
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000250"
SQ SEQUENCE 251 AA; 28459 MW; C4DCBB101FB2AC25 CRC64;
MLAELNAEVL ENTYISGNLY RLTLRIPDKI LKQIEPGHFA MIKPSDTYDP MGRRAFAVAD
IEEHKAVFYY DVYGKGTYLL SKRKPGERLK TFLPLGKRLF SYEGDKHLLI GGGVGLAGLT
LLAKKLRDMG KKVFIAYGGR SREHLGMVEW LEKEEFPYEL FTNDGSAGRK GFVTEILKEF
STDWVVHACG PKPMLKTIKE MKTGHKVYFS LEERMACGWG VCLGCVVKTR DGKFKRVCYE
GPVMPMEEVI L