(data stored in ACNUC29543 zone)

SWISSPROT: PYRC_SYNR3

ID   PYRC_SYNR3              Reviewed;         346 AA.
AC   A5GR03;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 68.
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=SynRCC307_0409;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl
CC       aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-dihydroorotate + H2O = H(+) + N-carbamoyl-L-
CC         aspartate; Xref=Rhea:RHEA:24296, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30864, ChEBI:CHEBI:32814;
CC         EC=3.5.2.3; 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
CC       pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00219}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00219}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. DHOase family. Class II DHOase subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00219}.
DR   EMBL; CT978603; CAK27312.1; -; Genomic_DNA.
DR   RefSeq; WP_011934827.1; NC_009482.1.
DR   SMR; A5GR03; -.
DR   STRING; 316278.SynRCC307_0409; -.
DR   PRIDE; A5GR03; -.
DR   EnsemblBacteria; CAK27312; CAK27312; SynRCC307_0409.
DR   KEGG; syr:SynRCC307_0409; -.
DR   eggNOG; ENOG4105EKE; Bacteria.
DR   eggNOG; COG0418; LUCA.
DR   HOGENOM; HOG000256259; -.
DR   KO; K01465; -.
DR   OMA; HLRDGAM; -.
DR   OrthoDB; 1319925at2; -.
DR   BioCyc; SSP316278:G1GJL-407-MONOMER; -.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000001115; 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; PS00483; DIHYDROOROTASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5GR03.
DR   SWISS-2DPAGE; A5GR03.
KW   Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis;
KW   Reference proteome; Zinc.
FT   CHAIN         1    346       Dihydroorotase.
FT                                /FTId=PRO_0000325579.
FT   REGION       19     21       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
FT   ACT_SITE    251    251       {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL        17     17       Zinc 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL        19     19       Zinc 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL       103    103       Zinc 1; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL       103    103       Zinc 2; via carbamate group.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL       140    140       Zinc 2; via pros nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL       178    178       Zinc 2; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   METAL       251    251       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
FT   BINDING      45     45       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
FT   BINDING     140    140       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
FT   BINDING     223    223       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
FT   BINDING     255    255       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
FT   BINDING     267    267       Substrate; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00219}.
FT   MOD_RES     103    103       N6-carboxylysine. {ECO:0000255|HAMAP-
FT                                Rule:MF_00219}.
SQ   SEQUENCE   346 AA;  38412 MW;  A71F7C06A5CCC1BA CRC64;
     MTPAPDQLVL RRPDDWHVHL RDDVMLEQVL PATARQFARA IVMPNLRPPV TTVDAAIAYR
     QRIEAALPDG MAFTPLMTAY LTDDISPDEL ERGHREGVFT AAKLYPANAT TNSAAGVSDL
     ACITAVLERM QAIDMPLLIH GEVTDPDIDI FDREAVFIER HLIPLRRQFP QLRVVFEHIT
     TEQAAQFVVD GDPLMAATIT PHHLHINRNA MFQGGLRSDF YCLPVAKRER HRLALRQAAT
     SGDPSFFLGT DSAPHPRAGK ESSCGCAGIY NAPYALESYL AVFEAEGALQ HFEAFASENG
     PRFYKLPLNE DTITLKRTAQ LVPAQLEGQG LVPFHASEVL DWRLAD
//

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