ID   RPIA_KLULA              Reviewed;         274 AA.
AC   Q6CTD5;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 92.
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; OrderedLocusNames=KLLA0C13541g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR382123; CAH01655.1; -; Genomic_DNA.
DR   RefSeq; XP_452804.1; XM_452804.1.
DR   AlphaFoldDB; Q6CTD5; -.
DR   SMR; Q6CTD5; -.
DR   STRING; 28985.XP_452804.1; -.
DR   EnsemblFungi; CAH01655; CAH01655; KLLA0_C13541g.
DR   GeneID; 2892283; -.
DR   KEGG; kla:KLLA0_C13541g; -.
DR   eggNOG; KOG3075; Eukaryota.
DR   HOGENOM; CLU_056590_0_0_1; -.
DR   InParanoid; Q6CTD5; -.
DR   OMA; YDWDEVN; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000000598; Chromosome C.
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   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:EnsemblFungi.
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..274
FT                   /note="Ribose-5-phosphate isomerase"
FT                   /id="PRO_0000339888"
SQ   SEQUENCE   274 AA;  29976 MW;  A61F9A4B3B3BDB28 CRC64;
     MYRVFDKLAS RPFVSLPGIQ LIAKMPLSDL NKLPPLADQL EQAKRIAAYR AVDENFDAKT
     HKVVGVGSGT TVVYVAERLG EYMDEKTNFV CIPTGFQSKQ LILSNKLQLG VIEQFPEVDI
     AFDGADEVDA GLQLIKGGGA CLFQEKLVST SAKKFIVVAD SRKKSPKYLG TNWKKGVPIE
     VVPSSYVRVL SDLKNKLNCK SAMVRQGGSA KAGPVVTDNC NFIIDADFGE ITDPRKLHQD
     IKLLVGVVET GLFIDNAEKA YFGYPDGSVD LQEL