PYRC_SULAC
ID PYRC_SULAC Reviewed; 389 AA.
AC O08357; Q4J8H3; Q8NKP6;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 123.
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=Saci_1593;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=12142413; DOI=10.1128/jb.184.16.4430-4441.2002;
RA Thia-Toong T.-L., Roovers M., Durbecq V., Gigot D., Glansdorff N.,
RA Charlier D.R.M.;
RT "Genes of de novo pyrimidine biosynthesis from the hyperthermoacidophilic
RT crenarchaeote Sulfolobus acidocaldarius: novel organization in a bipolar
RT operon.";
RL J. Bacteriol. 184:4430-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 35-389.
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RA Charlier D.R.M., Thia-Toong T.-L., Roovers M., Durbecq V., Legrain C.,
RA Glansdorff N.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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; AJ459777; CAD31979.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY80906.1; -; Genomic_DNA.
DR EMBL; Y12823; CAA73353.1; -; Genomic_DNA.
DR RefSeq; WP_011278408.1; NC_007181.1.
DR AlphaFoldDB; O08357; -.
DR SMR; O08357; -.
DR STRING; 330779.Saci_1593; -.
DR EnsemblBacteria; AAY80906; AAY80906; Saci_1593.
DR GeneID; 3474276; -.
DR KEGG; sai:Saci_1593; -.
DR PATRIC; fig|330779.12.peg.1533; -.
DR eggNOG; arCOG00689; Archaea.
DR HOGENOM; CLU_015572_1_1_2; -.
DR OMA; QHAQEPR; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000001018; 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; PS00482; DIHYDROOROTASE_1; 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..389
FT /note="Dihydroorotase"
FT /id="PRO_0000147279"
FT ACT_SITE 256
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 51
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 53..55
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 53
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 133
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 193
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 260
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 274..275
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT MOD_RES 133
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
SQ SEQUENCE 389 AA; 44248 MW; 2CDF3651B621A7C8 CRC64;
MWIKGKAYYE GEIKEICINF DRSIKEIRAN CKPDMTFTNE ELILPASVDL HVHVRGAQLS
YKETVATATS EAVYGGVGVI VDMPNTVPYI NTPERIKERL REFQLYSRTD YGIYSGVSKE
VEEIDKLPIA GYKIYPEDLE KEETRYVLEK SKKLKILHPE MPFVSKIERS LRRSYWMETA
AINLVKGNMH ITHITNFETL QLAKSMGFTT DITAHHLVVD GERDCISKVN PPIRDYVTRL
KLFLKGLFEV DCIASDHAPH SKEEKRMNFD LCPPGIAGVS FSTPYIYSLM FKGLISIDRA
VSLLSGNPSR ILNIPTGKIK EGYRANFTVI KRENWRYTTK FSKVTETPMD GFSLDAKVTN
VIVEGKLAFD GENVYPIRGV NIFDSSSRS
