(data stored in SCRATCH zone)

SWISSPROT: A0A0H2ZL93_PSEAB

ID   A0A0H2ZL93_PSEAB        Unreviewed;       423 AA.
AC   A0A0H2ZL93;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   30-AUG-2017, entry version 13.
DE   RecName: Full=Dihydroorotase {ECO:0000256|HAMAP-Rule:MF_00220};
DE            Short=DHOase {ECO:0000256|HAMAP-Rule:MF_00220};
DE            EC=3.5.2.3 {ECO:0000256|HAMAP-Rule:MF_00220};
GN   Name=pyrC {ECO:0000256|HAMAP-Rule:MF_00220,
GN   ECO:0000313|EMBL:ABJ15368.1};
GN   OrderedLocusNames=PA14_05250 {ECO:0000313|EMBL:ABJ15368.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15368.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15368.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15368.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
CC   -!- FUNCTION: Catalyzes the reversible cyclization of carbamoyl
CC       aspartate to dihydroorotate. {ECO:0000256|HAMAP-Rule:MF_00220}.
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L-
CC       aspartate. {ECO:0000256|HAMAP-Rule:MF_00220}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00220};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00220}.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases
CC       superfamily. DHOase family. Class I DHOase subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00220}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00220}.
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DR   EMBL; CP000438; ABJ15368.1; -; Genomic_DNA.
DR   RefSeq; WP_004365041.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZL93; -.
DR   EnsemblBacteria; ABJ15368; ABJ15368; PA14_05250.
DR   KEGG; pau:PA14_05250; -.
DR   KO; K01465; -.
DR   OMA; EYVKAFD; -.
DR   UniPathway; UPA00070; UER00117.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
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_type2_B; 1.
DR   InterPro; IPR006680; Amidohydro-rel.
DR   InterPro; IPR004722; DHOase.
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.
PE   3: Inferred from homology;
DR   PRODOM; A0A0H2ZL93.
DR   SWISS-2DPAGE; A0A0H2ZL93.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00220};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00220};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00220};
KW   Zinc {ECO:0000256|HAMAP-Rule:MF_00220}.
FT   DOMAIN      193    419       Amidohydro-rel. {ECO:0000259|Pfam:
FT                                PF01979}.
FT   REGION      324    325       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00220}.
FT   BINDING     310    310       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00220}.
SQ   SEQUENCE   423 AA;  44064 MW;  410D649818955EC1 CRC64;
     MTISIRGARV IDPASGLDQV GDLHIEAGKI VAIGAAPAGF SAQKTLDGAG LVAAPGLVDL
     SVALREPGYG RKGNVESETR AAAAGGTTSL CCPPYTRPVL DTPAVAELIL DRAREAGNAK
     VYPIGALTRG FGGEQLSELV ALRDTGCVAF TNGLHGFASN RILRRALEYA ATFDLTVIFT
     SQDTDLAEGG LAHEGPTASF LGLAGIPETA ETVALARNLL LVEQSGVRAH FSQLTSARGI
     ELVAQAQARG LPVTCDVALY QLILTDEALV GFSSLYHVQP PLRTKADREA LREAVKNGVV
     QAIASHHQPH EADAKNAPFA ATEPGISGAE LLLPLAMTLV QDGLLDLPTL LARLSHGPAQ
     ALRLPAGRLA VGQAADLVLF DPQGSTLAGE SWYSKGQNSP FVGHCLPGRV RYTLVDGHLT
     HEG
//

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