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PYRF_CANAL
ID   PYRF_CANAL              Reviewed;         270 AA.
AC   P13649; A0A1D8PJ56; Q5AJ76; Q9UVV6;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 4.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Orotidine 5'-phosphate decarboxylase;
DE            EC=4.1.1.23;
DE   AltName: Full=OMP decarboxylase;
DE            Short=OMPDCase;
DE            Short=OMPdecase;
DE   AltName: Full=Uridine 5'-monophosphate synthase;
DE            Short=UMP synthase;
GN   Name=URA3; OrderedLocusNames=CAALFM_C301350CA;
GN   ORFNames=CaO19.1716, CaO19.9284;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10231 / CBS 6431 / DSM 1386 / NBRC 1594;
RX   PubMed=2574635; DOI=10.1007/bf00391471;
RA   Ernst J.F., Losberger C.;
RT   "Sequence and transcript analysis of the C. albicans URA3 gene encoding
RT   orotidine-5'-phosphate decarboxylase.";
RL   Curr. Genet. 16:153-157(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1177;
RA   Hoyer L.L.;
RT   "Construction and evaluation of a Candida albicans gene expression
RT   cassette.";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + orotidine 5'-phosphate = CO2 + UMP;
CC         Xref=Rhea:RHEA:11596, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57538, ChEBI:CHEBI:57865; EC=4.1.1.23;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10110};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway;
CC       UMP from orotate: step 2/2.
CC   -!- SIMILARITY: Belongs to the OMP decarboxylase family. {ECO:0000305}.
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DR   EMBL; X14198; CAA32410.1; -; Genomic_DNA.
DR   EMBL; AF109400; AAF13298.1; -; Genomic_DNA.
DR   EMBL; CP017625; AOW28178.1; -; Genomic_DNA.
DR   PIR; A48331; DCCKA.
DR   RefSeq; XP_721787.2; XM_716694.2.
DR   AlphaFoldDB; P13649; -.
DR   SMR; P13649; -.
DR   STRING; 237561.P13649; -.
DR   GeneID; 3636649; -.
DR   KEGG; cal:CAALFM_C301350CA; -.
DR   CGD; CAL0000191638; URA3.
DR   VEuPathDB; FungiDB:C3_01350C_A; -.
DR   eggNOG; KOG1377; Eukaryota.
DR   HOGENOM; CLU_030821_0_0_1; -.
DR   InParanoid; P13649; -.
DR   OrthoDB; 1303452at2759; -.
DR   UniPathway; UPA00070; UER00120.
DR   PRO; PR:P13649; -.
DR   Proteomes; UP000000559; Chromosome 3.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IBA:GO_Central.
DR   GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR014732; OMPdecase.
DR   InterPro; IPR018089; OMPdecase_AS.
DR   InterPro; IPR001754; OMPdeCOase_dom.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR32119:SF2; PTHR32119:SF2; 1.
DR   Pfam; PF00215; OMPdecase; 1.
DR   SMART; SM00934; OMPdecase; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR01740; pyrF; 1.
DR   PROSITE; PS00156; OMPDECASE; 1.
PE   3: Inferred from homology;
KW   Decarboxylase; Lyase; Pyrimidine biosynthesis; Reference proteome.
FT   CHAIN           1..270
FT                   /note="Orotidine 5'-phosphate decarboxylase"
FT                   /id="PRO_0000134646"
FT   ACT_SITE        95
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10110"
FT   BINDING         39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         61..63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         93..102
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        81
FT                   /note="G -> E (in Ref. 1; CAA32410 and 2; AAF13298)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        184
FT                   /note="V -> I (in Ref. 1; CAA32410 and 2; AAF13298)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        257
FT                   /note="D -> N (in Ref. 1; CAA32410)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   270 AA;  29893 MW;  1B4FC3B48EBB727D CRC64;
     MTVNTKTYSE RAETHASPVA QRLFRLMESK KTNLCASIDV DTTKEFLELI DKLGPYVCLI
     KTHIDIINDF SYESTIEPLL GLSRKHQFMI FEDRKFADIG NTVKKQYIGG VYKISSWADI
     TNAHGVTGNG VVEGLKQGAK ETTTNQEPRG LLMLAELSSV GSLAYGEYSQ KTVEIAKSDK
     EFVVGFIAQR DMGGQEEGFD WLIMTPGVGL DDKGDGLGQQ YRTVDEVVST GTDIIIVGRG
     LFGKGRDPDI EGKRYRDAGW NAYLKKTGQL
 
 
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