PYRC_THEKO
ID PYRC_THEKO Reviewed; 409 AA.
AC Q5JJ91;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Dihydroorotase {ECO:0000255|HAMAP-Rule:MF_00220};
DE Short=DHOase {ECO:0000255|HAMAP-Rule:MF_00220};
DE EC=3.5.2.3 {ECO:0000255|HAMAP-Rule:MF_00220};
GN Name=pyrC {ECO:0000255|HAMAP-Rule:MF_00220}; OrderedLocusNames=TK1805;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
CC -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00220}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-aspartate;
CC Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30864, ChEBI:CHEBI:32814; EC=3.5.2.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00220};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00220};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00220};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000255|HAMAP-
CC Rule:MF_00220}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC DHOase family. Class I DHOase subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00220}.
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DR EMBL; AP006878; BAD85994.1; -; Genomic_DNA.
DR RefSeq; WP_011250756.1; NC_006624.1.
DR AlphaFoldDB; Q5JJ91; -.
DR SMR; Q5JJ91; -.
DR STRING; 69014.TK1805; -.
DR PRIDE; Q5JJ91; -.
DR EnsemblBacteria; BAD85994; BAD85994; TK1805.
DR GeneID; 3235573; -.
DR KEGG; tko:TK1805; -.
DR PATRIC; fig|69014.16.peg.1761; -.
DR eggNOG; arCOG00689; Archaea.
DR HOGENOM; CLU_015572_1_1_2; -.
DR InParanoid; Q5JJ91; -.
DR OMA; QHAQEPR; -.
DR OrthoDB; 43469at2157; -.
DR PhylomeDB; Q5JJ91; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_00220_A; PyrC_classI_A; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR004722; DHOase.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Pyrimidine biosynthesis; Reference proteome;
KW Zinc.
FT CHAIN 1..409
FT /note="Dihydroorotase"
FT /id="PRO_0000147278"
FT ACT_SITE 276
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 59..61
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 290..291
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT MOD_RES 139
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
SQ SEQUENCE 409 AA; 45471 MW; 5D16DA7A4701F00A CRC64;
MHELVLSGRF VLNGEIVGGS IGIDNGLITE ISRRDIKGEE VIAFKSEIIL PGLIDTHVHL
RDFEQKEKET VESGTKAALH GGITAVFDMP NTKPPIMDVK TFEKRLSILE KHAYSDYAAS
FLLAGNCGEA SRARADFYKI FMGASTGGIF SENFESDYSC APGIVSVHAE DPETIRENPE
RPPEAEIRAI KKALTAAEKL RKPLNVCHVS TVGGIEAIIK KNLPWVSFEV TPHHLFLTSK
DFERNPLLKV YPPLRSEEHR KALWENFSRI PIIASDHAPH TIEDKEAGAA GIPGLETEVA
LLLDAANRGL ITVFDIVEKM HDNPVRFFGI KGRDFSLGNE ATFTIIDPKK EWKVKPEEFY
TKAKWSPWEG KKLKGKVVMT VIRGMVVMEG DEIIEEPKGV RLDVQGGNH
