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PYRK_METTH
ID   PYRK_METTH              Reviewed;         266 AA.
AC   O27280;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 143.
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=MTH_1212;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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}.
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DR   EMBL; AE000666; AAB85701.1; -; Genomic_DNA.
DR   PIR; H69028; H69028.
DR   AlphaFoldDB; O27280; -.
DR   SMR; O27280; -.
DR   STRING; 187420.MTH_1212; -.
DR   PRIDE; O27280; -.
DR   EnsemblBacteria; AAB85701; AAB85701; MTH_1212.
DR   KEGG; mth:MTH_1212; -.
DR   PATRIC; fig|187420.15.peg.1190; -.
DR   HOGENOM; CLU_003827_1_1_2; -.
DR   OMA; RYMKCGI; -.
DR   UniPathway; UPA00070; UER00945.
DR   Proteomes; UP000005223; 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; PS00197; 2FE2S_FER_1; 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; Reference proteome; Transport.
FT   CHAIN           1..266
FT                   /note="Probable dihydroorotate dehydrogenase B (NAD(+)),
FT                   electron transfer subunit"
FT                   /id="PRO_0000148378"
FT   DOMAIN          5..99
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT   BINDING         217
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT   BINDING         222
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT   BINDING         225
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
FT   BINDING         235
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01211"
SQ   SEQUENCE   266 AA;  29773 MW;  F20A21D5E893A547 CRC64;
     MDSMNVPEVL EIKRIVEESE SVKTFIFSWD FRREVRPGQF VMVWDFRDEK PMSVSLIDPV
     RSEIGISIRR VGEFTDRVHG LSEGDLLGIR GPYGRGFELM GRDILLVGGG IGMAPLAALA
     DEATARGMRV DALVAARTAD ELLFLDRLEA AGVNISTCTD DGSCGFKGFA HERLLTLEEN
     HDMAAVCGPE PMMFQVMRIL DERDVPAQLS LERYMKCAVG ICGQCCLDDT GFRVCAEGPV
     FWSQELSRVR EFGRYRRDPA GRRVPW
 
 
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