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RPIA_YEAS7
ID   RPIA_YEAS7              Reviewed;         258 AA.
AC   A6ZNU5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=Ribose-5-phosphate isomerase;
DE            EC=5.3.1.6;
DE   AltName: Full=D-ribose-5-phosphate ketol-isomerase;
DE   AltName: Full=Phosphoriboisomerase;
GN   Name=RKI1; ORFNames=SCY_5163;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-ribose 5-phosphate = D-ribulose 5-phosphate;
CC         Xref=Rhea:RHEA:14657, ChEBI:CHEBI:58121, ChEBI:CHEBI:58273;
CC         EC=5.3.1.6;
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribose
CC       5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step
CC       1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; AAFW02000030; EDN63960.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZNU5; -.
DR   SMR; A6ZNU5; -.
DR   PRIDE; A6ZNU5; -.
DR   EnsemblFungi; EDN63960; EDN63960; SCY_5163.
DR   HOGENOM; CLU_056590_0_0_1; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:InterPro.
DR   CDD; cd01398; RPI_A; 1.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   InterPro; IPR004788; Ribose5P_isomerase_type_A.
DR   PANTHER; PTHR11934; PTHR11934; 1.
DR   Pfam; PF06026; Rib_5-P_isom_A; 1.
DR   SUPFAM; SSF100950; SSF100950; 1.
DR   TIGRFAMs; TIGR00021; rpiA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Isomerase.
FT   CHAIN           1..258
FT                   /note="Ribose-5-phosphate isomerase"
FT                   /id="PRO_0000339896"
SQ   SEQUENCE   258 AA;  28258 MW;  E9F72BF2759F4DDD CRC64;
     MAAGVPKIDA LESLGNPLED AKRAAAYRAV DENLKFDDHK IIGIGSGSTV VYVAERIGQY
     LHDPKFYEVA SKFICIPTGF QSRNLILDNK LQLGSIEQYP RIDIAFDGAD EVDENLQLIK
     GGGACLFQEK LVSTSAKTFI VVADSRKKSP KHLGKNWRQG VPIEIVPSSY VRVKNDLLEQ
     LHAEKVDIRQ GGSAKAGPVV TDNNNFIIDA DFGEISDPRK LHREIKLLVG VVETGLFIDN
     ASKAYFGNSD GSVEVTEK
 
 
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