PYRC_PYRAB
ID PYRC_PYRAB Reviewed; 404 AA.
AC Q9UXV6; G8ZKT5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 137.
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=PYRAB17520;
GN ORFNames=PAB1149;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248288; CAB50657.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE71226.1; -; Genomic_DNA.
DR PIR; C75027; C75027.
DR RefSeq; WP_010868871.1; NC_000868.1.
DR AlphaFoldDB; Q9UXV6; -.
DR SMR; Q9UXV6; -.
DR STRING; 272844.PAB1149; -.
DR EnsemblBacteria; CAB50657; CAB50657; PAB1149.
DR GeneID; 1496055; -.
DR KEGG; pab:PAB1149; -.
DR PATRIC; fig|272844.11.peg.1871; -.
DR eggNOG; arCOG00689; Archaea.
DR HOGENOM; CLU_015572_1_1_2; -.
DR OMA; QHAQEPR; -.
DR OrthoDB; 43469at2157; -.
DR PhylomeDB; Q9UXV6; -.
DR UniPathway; UPA00070; UER00117.
DR PRO; PR:Q9UXV6; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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; 2.
DR SUPFAM; SSF51338; SSF51338; 2.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Pyrimidine biosynthesis; Zinc.
FT CHAIN 1..404
FT /note="Dihydroorotase"
FT /id="PRO_0000147274"
FT ACT_SITE 272
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 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 135
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 164
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 276
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 286..287
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT MOD_RES 135
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
SQ SEQUENCE 404 AA; 45881 MW; C00D874AF77B7CDC CRC64;
MELVLVGKFL YNGRIIDGSI GVKDGKITKF SLRELKGDNK IKVEKGKIIL PGLIDVHVHL
RDFNETHKET IETGTKAAVH GGITTVFDMP NTKPPVMDEK TLKMREFLFK KKSYADYALG
FLLAGNEPVK ADFYKIFMGA STGGIYSKNF EEDYAKALDI TSVHAEDYEL ISKYPERPPI
VEISAIKKAL NAARKVKKPL HICHVSTREG LKEILEANIP WVSFEVTPHH LFLTRKDYEK
SKLLKVYPPL RDESDRRYLW EKLDNVPIIA SDHAPHTLED KERGAAGLPG LETEVALLLD
AVNRGMLELW DVVEKMSLNP ARIFRIKNKG WGEGKDADFA IVDMKKEWTI KAEEFYTKAG
WTPYEGWKVR GKVIMTILRG EIVMEDDEVI GKPRGERIVK EGDD
