PYRC_SHEB9
ID PYRC_SHEB9 Reviewed; 343 AA.
AC A9L3F5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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};
GN OrderedLocusNames=Sbal195_1028;
OS Shewanella baltica (strain OS195).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=399599;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS195;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Brettar I.,
RA Rodrigues J., Konstantinidis K., Klappenbach J., Hofle M., Tiedje J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS195.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000891; ABX48204.1; -; Genomic_DNA.
DR RefSeq; WP_006085865.1; NC_009997.1.
DR AlphaFoldDB; A9L3F5; -.
DR SMR; A9L3F5; -.
DR EnsemblBacteria; ABX48204; ABX48204; Sbal195_1028.
DR GeneID; 11771318; -.
DR KEGG; sbn:Sbal195_1028; -.
DR HOGENOM; CLU_041558_1_0_6; -.
DR OMA; TLHHISM; -.
DR UniPathway; UPA00070; UER00117.
DR Proteomes; UP000000770; 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..343
FT /note="Dihydroorotase"
FT /id="PRO_1000078103"
FT ACT_SITE 247
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 13
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 15..17
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 15
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 41
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 99
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 99
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 136
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 247
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT BINDING 263
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
FT MOD_RES 99
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00219"
SQ SEQUENCE 343 AA; 37729 MW; 36B79F3B011B2DE4 CRC64;
MTTITITRPD DWHIHLRDGA QLKDTVRDIS RYMGRAIVMP NLVPPAIDTE TALTYYDRIK
AQVPAGSQFE PLMVLYLTDK TSPDEIRRAK ASGKIVAAKL YPAGATTNSD SGVTDLKNIY
PALEAMQEVG MLFLVHGEVT DSSIDIFDRE RVFIENILSK IVADFPELKI VLEHITTKDA
VDFVTQASDN VAATITAHHL LYNRNHMLAG GIRPHFYCLP ILKRNTHQQA LLAAAASGSK
KFFLGTDSAP HAKDKKEAAC GCAGSYTAHA AIELYAEAFE SVNALDKLEA FASFNGPDFY
NLPRNADTIT LVKKPWNVPA TYPLGDTNVV PIRAGEAIDW QVE
