PYRK_THEVO
ID PYRK_THEVO Reviewed; 250 AA.
AC Q979G5;
DT 11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Probable dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit {ECO:0000255|HAMAP-Rule:MF_01211};
DE AltName: Full=Dihydroorotate oxidase B, electron transfer subunit {ECO:0000255|HAMAP-Rule:MF_01211};
GN Name=pyrK {ECO:0000255|HAMAP-Rule:MF_01211}; OrderedLocusNames=TV1196;
GN ORFNames=TVG1225518;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
CC -!- FUNCTION: Responsible for channeling the electrons from the oxidation
CC of dihydroorotate from the FMN redox center in the PyrD type B subunit
CC to the ultimate electron acceptor NAD(+). {ECO:0000255|HAMAP-
CC Rule:MF_01211}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01211};
CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01211};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01211};
CC Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01211};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_01211}.
CC -!- SUBUNIT: Heterotetramer of 2 PyrK and 2 PyrD type B subunits.
CC {ECO:0000255|HAMAP-Rule:MF_01211}.
CC -!- SIMILARITY: Belongs to the PyrK family. {ECO:0000255|HAMAP-
CC Rule:MF_01211}.
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; BA000011; BAB60338.1; -; Genomic_DNA.
DR RefSeq; WP_010917429.1; NC_002689.2.
DR AlphaFoldDB; Q979G5; -.
DR SMR; Q979G5; -.
DR STRING; 273116.14325434; -.
DR DNASU; 1441311; -.
DR EnsemblBacteria; BAB60338; BAB60338; BAB60338.
DR GeneID; 1441311; -.
DR KEGG; tvo:TVG1225518; -.
DR eggNOG; arCOG02199; Archaea.
DR HOGENOM; CLU_003827_1_1_2; -.
DR OMA; RYMKCGI; -.
DR OrthoDB; 67226at2157; -.
DR PhylomeDB; Q979G5; -.
DR UniPathway; UPA00070; UER00945.
DR Proteomes; UP000001017; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0009055; F:electron transfer activity; IEA:UniProtKB-UniRule.
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:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.10.240.10; -; 1.
DR Gene3D; 3.40.50.80; -; 1.
DR HAMAP; MF_01211; DHODB_Fe_S_bind; 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; IPR023455; Dihydroorotate_DHASE_ETsu.
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; Pyrimidine biosynthesis; Transport.
FT CHAIN 1..250
FT /note="Probable dihydroorotate dehydrogenase B (NAD(+)),
FT electron transfer subunit"
FT /id="PRO_0000148384"
FT DOMAIN 1..89
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT BINDING 200
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT BINDING 205
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT BINDING 208
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT BINDING 216
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
SQ SEQUENCE 250 AA; 28121 MW; 1D918B9CE93CC451 CRC64;
MINLKIEENV KESQNVNTLY FNWDQDIRPG QFAMIWIPGY GEIPMSFSGL GRRKSITVKA
YGSASRKLTE LKAGDDLFLR GPYGNGFDVR EGRKLLVGGG SGIVSLYPIA DQETDALISA
KTRDELIFKD RFPESRRFIA TDDGSDGFHG FAHELLQRIN IDSYEAIYVC GPEQMMYKVL
QVLKGRKVFV QFSLERTMKC GIGICDSCSL GGKQVCKEGP VFNIEELIGN PEFGVYRTTY
SGRRIRLNVK
