(data stored in ACNUC7421 zone)

HOGENOM: SHIF8_1_PE1005

ID   SHIF8_1_PE1005                       STANDARD;      PRT;   348 AA.
AC   SHIF8_1_PE1005; Q0T5X0;
DT   00-JAN-0000 (Rel. 1, Created)
DT   00-JAN-0000 (Rel. 2, Last sequence update)
DT   00-JAN-0000 (Rel. 3, Last annotation update)
DE   RecName: Full=Dihydroorotase; Short=DHOase; EC=3.5.2 3; (SHIF8_1.PE1005).
GN   Name=pyrC; OrderedLocusNames=SFV_1084;
OS   SHIGELLA FLEXNERI 5 STR. 8401.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=373384;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS SHIF8_1.PE1005.
CC       Shigella flexneri 5 str. 8401, complete genome.
CC       sequence.
CC   -!- ANNOTATIONS ORIGIN:PYRC_SHIF8
CC   -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L-
CC       aspartate.
CC   -!- COFACTOR: Binds 2 zinc ions per subunit (By similarity).
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 3/3.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the DHOase family. Type 1 subfamily.
CC   -!- GENE_FAMILY: HOG000256259 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q0T5X0; -.
DR   EMBL; CP000266; ABF03295.1; -; Genomic_DNA.
DR   RefSeq; YP_688600.1; NC_008258.1.
DR   ProteinModelPortal; Q0T5X0; -.
DR   SMR; Q0T5X0; 5-347.
DR   STRING; Q0T5X0; -.
DR   EnsemblBacteria; EBESCT00000097205; EBESCP00000093401; EBESCG00000096249.
DR   GeneID; 4209566; -.
DR   GenomeReviews; CP000266_GR; SFV_1084.
DR   KEGG; sfv:SFV_1084; -.
DR   eggNOG; COG0418; -.
DR   GeneTree; EBGT00050000011208; -.
DR   OMA; CLPVAKR; -.
DR   ProtClustDB; PRK05451; -.
DR   BioCyc; SFLE373384:SFV_1084-MON; -.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019856; P:pyrimidine base biosynthetic process; IEA:InterPro.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00219; PyrC_type1; 1; -.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR004721; DHOdimr.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   PIRSF; PIRSF001237; DHOdimr; 1.
DR   TIGRFAMs; TIGR00856; PyrC_dimer; 1.
DR   PROSITE; PS00482; DIHYDROOROTASE_1; 1.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
DR   HOGENOMDNA; SHIF8_1.PE1005; -.
KW   Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis;
KW   Zinc.
SQ   SEQUENCE   348 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MTAPSQVLKI RRPDDWHLHL RDGDMLKTVV PYTSEIYGRA IVMPNLAPPV TTVEAAVAYR
     QRILDAVPAG HDFTPLMTCY LTDSLDPNEL ERGFNEAVFT AAKLYPANAT TNSSHGVTSI
     DAIMPVLERM EKIGMPLLVH GEVTHADIDI FDREARFIES VMEPLRQRLT ALKVVFEHIT
     TKDAADYVRD GNERLAATIT PQHLMFNRNH MLVGGVRPHL YCLPILKRNI HQQALRELVT
     SGFNRVFLGT DSAPHARHRK ESSCGCAGCF NAPTALGSYA TVFEEMNALQ HFEAFCSVNG
     PQFYGLPVND TFIELVREEQ QVAESIALTD DTLVPFLAGE TVRWSVKQ
//

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