GenomeNet

Database: UniProt
Entry: P48795
LinkDB: P48795
Original site: P48795 
ID   PYRC_LACLE              Reviewed;         427 AA.
AC   P48795;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   30-AUG-2017, entry version 88.
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};
OS   Lactobacillus leichmannii.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=28039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 4797 / DSM 20076 / JCM 1148 / NCIB 7854 / F59 / 326;
RX   PubMed=8589056; DOI=10.1016/0300-9084(96)88135-1;
RA   Schenk-Groeninger R., Becker J., Brendel M.;
RT   "Cloning, sequencing, and characterizing the Lactobacillus leichmannii
RT   pyrC gene encoding dihydroorotase.";
RL   Biochimie 77:265-272(1995).
CC   -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl
CC       aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00220}.
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L-
CC       aspartate. {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
CC       pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
CC       {ECO:0000255|HAMAP-Rule:MF_00220}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. DHOase family. Class I DHOase subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00220}.
DR   EMBL; X78999; CAA55633.1; -; Genomic_DNA.
DR   PIR; T46955; T46955.
DR   ProteinModelPortal; P48795; -.
DR   SMR; P48795; -.
DR   UniPathway; UPA00070; UER00117.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 2.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   TIGRFAMs; TIGR00857; pyrC_multi; 1.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Pyrimidine biosynthesis; Zinc.
FT   CHAIN         1    427       Dihydroorotase.
FT                                /FTId=PRO_0000147236.
FT   REGION       60     62       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   REGION      321    322       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   ACT_SITE    303    303       {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL        58     58       Zinc 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL        60     60       Zinc 1; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL       150    150       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   METAL       150    150       Zinc 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   METAL       177    177       Zinc 2; via pros nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL       230    230       Zinc 2; via tele nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00220}.
FT   METAL       303    303       Zinc 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   BINDING      92     92       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   BINDING     276    276       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
FT   BINDING     307    307       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00220}.
SQ   SEQUENCE   427 AA;  46319 MW;  1AB5BC6163C57E30 CRC64;
     MAILLKNGLV YQEGEFIKED VLISGSKIQA IGLDLPEEGA EVYDLKGKLL APGLVDIHEH
     YREPGFTYKE TIKTGSEAAS RGGFTTVCTM PNVDPIPDDL ETFEKQVALN EANSCVHLKQ
     YGAITEDLTS DKVVDMAALK EAGAFAFSND GHGIQQAGTM YEAMQEAAKV GLAICEHIQD
     DSLYHHGVMN AGKKAEELGL PGILGVSESA QLARDLVLAQ ATGVHYHACH VSTKESVELI
     RIAKEYGINV TAEATPHHLL LSEEEIDGNN GYYKMNPPLR SKEDQFALIE GMLDGTIDLI
     ATDHAPHSRE EKAGDMRKAA FGIIGNETAF ACLYTKFVKS GQMDLSLLLD LMSYQPAKLF
     GLDAGVLAPG KEADLAVFDL DHAEKLSEED YLSKGVNTPF TGQEVYGMTA LTFVSGKLVY
     KSKHFAD
//
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