PYRC_CARHZ
ID PYRC_CARHZ Reviewed; 430 AA.
AC Q3AC01;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=CHY_1501;
OS Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 /
OS Z-2901).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Carboxydothermus.
OX NCBI_TaxID=246194;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-161 / DSM 6008 / Z-2901;
RX PubMed=16311624; DOI=10.1371/journal.pgen.0010065;
RA Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J.,
RA Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J.,
RA Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.;
RT "Life in hot carbon monoxide: the complete genome sequence of
RT Carboxydothermus hydrogenoformans Z-2901.";
RL PLoS Genet. 1:563-574(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; CP000141; ABB14270.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3AC01; -.
DR SMR; Q3AC01; -.
DR STRING; 246194.CHY_1501; -.
DR EnsemblBacteria; ABB14270; ABB14270; CHY_1501.
DR KEGG; chy:CHY_1501; -.
DR eggNOG; COG0044; Bacteria.
DR HOGENOM; CLU_015572_1_0_9; -.
DR OMA; QHAQEPR; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000002706; 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 CDD; cd01317; DHOase_IIa; 1.
DR Gene3D; 2.30.40.10; -; 1.
DR HAMAP; MF_00220_B; PyrC_classI_B; 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..430
FT /note="Dihydroorotase"
FT /id="PRO_1000024079"
FT ACT_SITE 304
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 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 304
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 308
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
FT BINDING 322..323
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00220"
SQ SEQUENCE 430 AA; 47093 MW; 0CA0F06BA9EB2890 CRC64;
MGMLIKNGNV VMVEDGKIRK MDVLIDKGII VEISPEINRS DVEVIDIEGK FLIPGLIDMH
VHFRDPGYTH KEDIHSGSNA ALAGGFTGVL MMPNTDPPPD NATVIYYWKE KSKSIPLNIL
FSGCITKNRA GKELSKFYEL KEAGAVAITD DGNWVADGAV FRHAMEYAAA LDLLVITHPE
EPTIANRGVI NEGYWSTVLG LRGIPKAAEN IAIYRDIEIA KMTGAKLHVA HLSTAEGVRL
VAAAKKLGLK VTAEVTPHHL VLTDEALAGY DTNLKVNPPL REAEEQKALL KGLLEGVIDV
IATDHAPHAS YEKNVEFNDA PFGIEGLETA FPVLYTELVL KKKITLEKLL LKMTVNPAKI
LQLPKQGDIK KGNYANLTVI DPKLTLKVSE ELLVGKSKNN PFLGRTLTGW PVMTVYQGIV
AYQRLLKGVQ
