ID   RPIA_PICGU              Reviewed;         247 AA.
AC   A5DFH6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   25-MAY-2022, entry version 68.
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=PGUG_02027;
OS   Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS   / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX   NCBI_TaxID=294746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH408156; EDK37929.2; -; Genomic_DNA.
DR   RefSeq; XP_001486356.1; XM_001486306.1.
DR   AlphaFoldDB; A5DFH6; -.
DR   SMR; A5DFH6; -.
DR   STRING; 4929.XP_001486356.1; -.
DR   EnsemblFungi; EDK37929; EDK37929; PGUG_02027.
DR   GeneID; 5127693; -.
DR   KEGG; pgu:PGUG_02027; -.
DR   eggNOG; KOG3075; Eukaryota.
DR   HOGENOM; CLU_056590_0_0_1; -.
DR   InParanoid; A5DFH6; -.
DR   OMA; YDWDEVN; -.
DR   OrthoDB; 1074761at2759; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000001997; 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; Reference proteome.
FT   CHAIN           1..247
FT                   /note="Ribose-5-phosphate isomerase"
FT                   /id="PRO_0000339890"
SQ   SEQUENCE   247 AA;  26395 MW;  40649B4CC930B2D2 CRC64;
     MLPTFVRFSR IMSSGIEHAK RMAAYKAVDA NFPPHAKVVG IGSGSTVVYV AERIGQLKNK
     HDFVCISTGF QSKQLIIDNG LTLGAIEQFP KVDIAFDGAD EVDTNLNLIK GGGACLFQEK
     LVASSADKFI VVADTRKKSP SDLGIAWRKG VPIEVVPNSY AVVTRQLKEL GAKSVVLRQG
     GGAKAGPVVT DNNNFLIDAD FGSISDPGSL HQQIKLLVGV VETGLFVDMA HTAYFGDESG
     EVSEQSR