PYRC_PSEPF
ID PYRC_PSEPF Reviewed; 348 AA.
AC Q3K7J8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Dihydroorotase {ECO:0000255|HAMAP-Rule:MF_00219};
DE Short=DHOase {ECO:0000255|HAMAP-Rule:MF_00219};
DE EC=3.5.2.3 {ECO:0000255|HAMAP-Rule:MF_00219};
GN Name=pyrC {ECO:0000255|HAMAP-Rule:MF_00219}; OrderedLocusNames=Pfl01_4519;
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(2009).
CC -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate
CC to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.
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_00219};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00219};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00219};
CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC (S)-dihydroorotate from bicarbonate: step 3/3. {ECO:0000255|HAMAP-
CC Rule:MF_00219}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00219}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC DHOase family. Class II DHOase subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00219}.
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DR EMBL; CP000094; ABA76256.1; -; Genomic_DNA.
DR RefSeq; WP_011335738.1; NC_007492.2.
DR AlphaFoldDB; Q3K7J8; -.
DR SMR; Q3K7J8; -.
DR STRING; 205922.Pfl01_4519; -.
DR MEROPS; M38.A02; -.
DR PRIDE; Q3K7J8; -.
DR EnsemblBacteria; ABA76256; ABA76256; Pfl01_4519.
DR KEGG; pfo:Pfl01_4519; -.
DR eggNOG; COG0418; Bacteria.
DR HOGENOM; CLU_041558_1_0_6; -.
DR OMA; TLHHISM; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000002704; 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 GO; GO:0019856; P:pyrimidine nucleobase biosynthetic process; IEA:InterPro.
DR CDD; cd01294; DHOase; 1.
DR HAMAP; MF_00219; PyrC_classII; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR004721; DHOdimr.
DR InterPro; IPR002195; Dihydroorotase_CS.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR43137; PTHR43137; 1.
DR Pfam; PF01979; Amidohydro_1; 1.
DR PIRSF; PIRSF001237; DHOdimr; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR00856; pyrC_dimer; 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..348
FT /note="Dihydroorotase"
FT /id="PRO_1000024038"
FT ACT_SITE 248
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 14
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 16..18
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 42
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /note="via carbamate group"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 137
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 175
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 252
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT MOD_RES 100
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
SQ SEQUENCE 348 AA; 38480 MW; AB078C90E2570A7E CRC64;
MSDRLTLLRP DDWHIHLRDG AVLTNTVADV ARTFGRAIIM PNLVPPVRNA AEADGYRQRI
LAARPAGSRF EPLMVLYLTD RTQPEEIREA KASGFVHAAK LYPAGATTNS DSGVTSIDKI
FPVLEAMAEA GMPLLIHGEV TRGDVDVFDR EKIFIDEHMR RVVERFPTLK VVFEHITTGD
AVQFVNEASA NVGATITAHH LLYNRNHMLV GGIRPHFYCL PILKRNTHQE ALLDAATSGS
AKFFLGTDSA PHAQHAKEAA CGCAGCYTAY AAIELYAEAF EQRNALDKLE AFASLNGPRF
YGLPANTDRI TLVRDEWTAP TSLPFGELTV IPLRAGEKLR WRLLEEHA
