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PYRC_PYRHO
ID   PYRC_PYRHO              Reviewed;         417 AA.
AC   O57740;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 131.
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=PH1963;
GN   ORFNames=PHBD037;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
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; BA000001; BAA31090.1; -; Genomic_DNA.
DR   PIR; C71212; C71212.
DR   AlphaFoldDB; O57740; -.
DR   SMR; O57740; -.
DR   STRING; 70601.3258407; -.
DR   EnsemblBacteria; BAA31090; BAA31090; BAA31090.
DR   KEGG; pho:PH1963; -.
DR   eggNOG; arCOG00689; Archaea.
DR   OMA; QHAQEPR; -.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000000752; 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..417
FT                   /note="Dihydroorotase"
FT                   /id="PRO_0000147277"
FT   ACT_SITE        275
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         62..64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         62
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         207
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         275
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         279
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   BINDING         289..290
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT   MOD_RES         138
FT                   /note="N6-carboxylysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
SQ   SEQUENCE   417 AA;  47226 MW;  733DF7E87F55394B CRC64;
     MTQVDLVVVG KFLFKEKIID GSIGIEDDKI AKFSLRELKG DKKIKVEKGK IILPGLIDVH
     VHLRDFNESY KETIASGTKA AIHGGITTVF DMPNTKPPIM DEKTLKLREL IFKKKSYSDY
     ALGFLIAGNE PAKADFYKIF MGASTGGIYS KNFEEDYKKA PDIVSVHAEE YELINRYPER
     PPIVEVVAIK KALQASKKMK KPLHICHVST KDGLKEILKA NIPWVSFEVT PHHLFLTRRD
     YERSKLLKVY PPLRDEEDRR YLWENLKSIP IIASDHAPHT LEDKEAGAAG LPGLETEVAL
     LLDAVNKGMI TIWDIVAKMS INPARIFKIK NKGWEEGKDA DLIVVDMKKE WTIKAENFYT
     KANWTPYEGW KVKGKVIMTI LRGEVVMEDD EIIGKPRGER IVKEGNAQGN LGSSQEH
 
 
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