(data stored in SCRATCH zone)

HOGENOM: FUNUC1_1_PE1000

ID   FUNUC1_1_PE1000                      STANDARD;      PRT;   425 AA.
AC   FUNUC1_1_PE1000; Q8RG88;
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;
DE   (FUNUC1_1.PE1000).
GN   Name=pyrC; OrderedLocusNames=FN0420;
OS   FUSOBACTERIUM NUCLEATUM SUBSP. NUCLEATUM ATCC 25586.
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [0]
RP   -.;
RG   -.;
RL   -.;
CC   -!- SEQ. DATA ORIGIN: Translated from the HOGENOM CDS FUNUC1_1.PE1000.
CC       Fusobacterium nucleatum subsp. nucleatum ATCC 25586 chromosome, complet
CC       genome.
CC   -!- ANNOTATIONS ORIGIN:PYRC_FUSNN
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 2 subfamily.
CC   -!- GENE_FAMILY: HOG000219142 [ FAMILY / ALN / TREE ]
DR   UniProtKB/Swiss-Prot; Q8RG88; -.
DR   EMBL; AE009951; AAL94623.1; -; Genomic_DNA.
DR   RefSeq; NP_603324.1; NC_003454.1.
DR   ProteinModelPortal; Q8RG88; -.
DR   GeneID; 992862; -.
DR   GenomeReviews; AE009951_GR; FN0420.
DR   KEGG; fnu:FN0420; -.
DR   NMPDR; fig|190304.1.peg.1003; -.
DR   OMA; PSICEST; -.
DR   ProtClustDB; PRK09357; -.
DR   BioCyc; FNUC190304:FN0420-MON; -.
DR   GO; GO:0004151; F:dihydroorotase activity; IEA:EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR   HAMAP; MF_00220_B; PyrC_type2_B; 1; -.
DR   InterPro; IPR006680; Amidohydro_1.
DR   InterPro; IPR004722; DHOase.
DR   InterPro; IPR002195; Dihydroorotase_CS.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   Pfam; PF01979; Amidohydro_1; 1.
DR   SUPFAM; SSF51338; Metalo_hydrolase; 1.
DR   TIGRFAMs; TIGR00857; PyrC_multi; 1.
DR   PROSITE; PS00482; DIHYDROOROTASE_1; FALSE_NEG.
DR   PROSITE; PS00483; DIHYDROOROTASE_2; 1.
DR   HOGENOMDNA; FUNUC1_1.PE1000; -.
KW   Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis;
KW   Reference proteome; Zinc.
SQ   SEQUENCE   425 AA;  UNKNOWN MW;  UNKNOWN CRC64;
     MLLKNCKILK NTKFEKVDIL IRDNKIEKIS ENIDITDENI IDIKNRFVTA GFIDVHVHWR
     EPGFSKKETV YTASRAAARG GFTTVMTMPN LNPVPDSVET LNKQLEIIKK DSVIRAIPYG
     AITKEEYGRE LSDMEAIASN VFAFTDDGRG VQSANVMYEA MLMGAKLNKA IVAHCEDNSL
     IRGGAMHEGK RSAELGIKGI PSICESTQIV RDVLLAEAAN CHYHVCHISA KESVRAVREG
     KKNGIKVTCE VTPHHLLSCD EDIKEDNGMW KMNPPLRSRE DRNALIVGIL DGTIDIIATD
     HAPHTMEEKI RGIEKSSFGI VGSETAFAQL YTKFVKTDIF SLEMLVKLMS ENVAKIFDLP
     YGKLEENSFA DIVVIDLEKE ITINPNNFLS KGKNTPYINE KINGIPVLTI SNGKIAYIDK
     EEINL
//

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