ID PYRC_PYRAE Reviewed; 383 AA.
AC Q8ZZC7;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 113.
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=PAE0322;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL62714.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZZC7; -.
DR SMR; Q8ZZC7; -.
DR STRING; 178306.PAE0322; -.
DR EnsemblBacteria; AAL62714; AAL62714; PAE0322.
DR KEGG; pai:PAE0322; -.
DR PATRIC; fig|178306.9.peg.245; -.
DR eggNOG; arCOG00689; Archaea.
DR HOGENOM; CLU_015572_1_1_2; -.
DR InParanoid; Q8ZZC7; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000002439; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004038; F:allantoinase activity; IBA:GO_Central.
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 GO; GO:0006145; P:purine nucleobase catabolic process; IBA:GO_Central.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
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 PANTHER; PTHR43668; ALLANTOINASE; 1.
DR PANTHER; PTHR43668:SF2; ALLANTOINASE; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 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..383
FT /note="Dihydroorotase"
FT /id="PRO_0000147275"
FT ACT_SITE 264
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 49..51
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 49
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 128
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 268
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 280..281
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT MOD_RES 128
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
SQ SEQUENCE 383 AA; 42421 MW; C51F4FD2B0EA3A52 CRC64;
MLKECIKIEG RAFLGGKVTR VKLGSGECKT LQLSNKYLIL PGMVDIHVHF RDWGLSHKET
LRGGAAAALA GGVVAVGDMP NTKPHIRTAD LYKKRLEEGS ALPIIYKVHM GIPQDLEELR
AARPPTIKIY PEDVEAFGWG HIEKAAEACA SLGCRLVLHC EDPAYFKEGE RPPIAELACV
ERTRQMAFKT GVKIHLTHIT LSQTAEAARG WATVDATPHH LLLDVENCKD SGLCHVNPRL
RTPEMRKRLL AAFASGLVDI YATDHAPHTL EEKRSGAPPP GICSLDVALS LLLTLWKRGV
VTLSDVVRLY SHRPARFFDL QIDVKKGYFT VVRLEEFTVR GEEFAGTCKH TPFEGFKAFG
RVFATSVGGR IYFKDGDVYM INI
//
