ID   RPIA_LODEL              Reviewed;         284 AA.
AC   A5DXV6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 72.
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=LELG_02193;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
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; CH981525; EDK44014.1; -; Genomic_DNA.
DR   RefSeq; XP_001527364.1; XM_001527314.1.
DR   AlphaFoldDB; A5DXV6; -.
DR   SMR; A5DXV6; -.
DR   STRING; 379508.A5DXV6; -.
DR   EnsemblFungi; EDK44014; EDK44014; LELG_02193.
DR   GeneID; 5234425; -.
DR   KEGG; lel:LELG_02193; -.
DR   VEuPathDB; FungiDB:LELG_02193; -.
DR   eggNOG; KOG3075; Eukaryota.
DR   HOGENOM; CLU_056590_0_0_1; -.
DR   InParanoid; A5DXV6; -.
DR   OMA; YDWDEVN; -.
DR   OrthoDB; 1074761at2759; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000001996; 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..284
FT                   /note="Ribose-5-phosphate isomerase"
FT                   /id="PRO_0000339889"
SQ   SEQUENCE   284 AA;  30972 MW;  E9E76D10CDCB6743 CRC64;
     MLFHRILPQY KTAISTYLTP THCRLYIANL VTSRRMTNIE AAKKLAAYRA VDENLPPHAK
     VIGIGSGSTV VYVAERIGQL PNKDDFVCIS TGFQSKQLII DNGLKLGQIE QHPSIDIAFD
     GADEVDPQLN LIKGGGACLF QEKLVASASD KLIIVADFRK QSKHLGQNWR QGVPIEVVPI
     AFTKLINDLK RLGAKSVDLR QGGKAKAGPV ITDNNNFILD ADFGIIEDPK SLHLQLKQLV
     GVVDTGLFTG ITEKVYFGEE SGEVTTWDGV VTGSTTEEVI AESK