ID   PYRK_THEMA              Reviewed;         217 AA.
AC   Q9WYG9;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Putative dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit;
DE   AltName: Full=Dihydroorotate oxidase B, electron transfer subunit;
GN   Name=pyrK; OrderedLocusNames=TM_0334;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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:0000250}.
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   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       orotate from (S)-dihydroorotate (NAD(+) route): step 1/1.
CC   -!- SUBUNIT: Heterotetramer of 2 PyrK and 2 PyrD type B subunits.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PyrK family. {ECO:0000305}.
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DR   EMBL; AE000512; AAD35421.1; -; Genomic_DNA.
DR   PIR; H72390; H72390.
DR   RefSeq; NP_228145.1; NC_000853.1.
DR   RefSeq; WP_010865096.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9WYG9; -.
DR   SMR; Q9WYG9; -.
DR   STRING; 243274.THEMA_03050; -.
DR   EnsemblBacteria; AAD35421; AAD35421; TM_0334.
DR   KEGG; tma:TM0334; -.
DR   KEGG; tmw:THMA_0342; -.
DR   PATRIC; fig|243274.18.peg.595; -.
DR   eggNOG; COG0543; Bacteria.
DR   OMA; LNEYMAC; -.
DR   OrthoDB; 1885467at2; -.
DR   UniPathway; UPA00070; UER00945.
DR   Proteomes; UP000008183; 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:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.10.240.10; -; 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; 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.
PE   3: Inferred from homology;
KW   2Fe-2S; Electron transport; FAD; Flavoprotein; Iron; Iron-sulfur;
KW   Metal-binding; Pyrimidine biosynthesis; Reference proteome; Transport.
FT   CHAIN           1..217
FT                   /note="Putative dihydroorotate dehydrogenase B (NAD(+)),
FT                   electron transfer subunit"
FT                   /id="PRO_0000409560"
FT   BINDING         66..67
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         183
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         188
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
FT   BINDING         203
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   217 AA;  24474 MW;  27A0570EA5CF6540 CRC64;
     MERLLLTKKK TIRVNEDTWI VLFEERIDFS PGQFVMLETP KLVRKPFVLG YWEDHTAISV
     QVKGKGTKWI VEEAEKIKGH GPLGNGFEKP GKGLLIISPT CLTMAEAFRK KMNVDVLVGS
     RTPFQIPLDH ETAVGDEEFL SKLSSTGEYD WYLVSGSRGM EKVCWEHLKG KEVYFSLEEY
     MGCGIGACKS CAVFTKEGVK HVCTDGPIFR GDELCWS