ID   RPIA_DEBHA              Reviewed;         252 AA.
AC   Q6BYI4;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 88.
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=DEHA2A09328g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382133; CAG84694.2; -; Genomic_DNA.
DR   RefSeq; XP_456735.2; XM_456735.2.
DR   AlphaFoldDB; Q6BYI4; -.
DR   SMR; Q6BYI4; -.
DR   STRING; 4959.XP_456735.2; -.
DR   EnsemblFungi; CAG84694; CAG84694; DEHA2A09328g.
DR   GeneID; 2899730; -.
DR   KEGG; dha:DEHA2A09328g; -.
DR   VEuPathDB; FungiDB:DEHA2A09328g; -.
DR   eggNOG; KOG3075; Eukaryota.
DR   HOGENOM; CLU_056590_0_0_1; -.
DR   InParanoid; Q6BYI4; -.
DR   OMA; YDWDEVN; -.
DR   OrthoDB; 1074761at2759; -.
DR   UniPathway; UPA00115; UER00412.
DR   Proteomes; UP000000599; Chromosome A.
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..252
FT                   /note="Ribose-5-phosphate isomerase"
FT                   /id="PRO_0000339887"
SQ   SEQUENCE   252 AA;  27289 MW;  754873F4C9E5B969 CRC64;
     MLKRIISARY IRNMSSGASL VEKAKKSAAY QAVDENFPEG AKVVGVGSGS TVIYVAERIS
     QLKNKESFVC VPTGFQSKQL IIDAGLRLGT IEQYPEVDIA FDGADEVDTE LNLIKGGGAC
     LFQEKLVAAA ASKFVIVADF RKRSPSKLGI QWRKGVPIEI VPCAYAKVSK DLEAMGAKKV
     ELRQGGSAKA GPVVTDNNNF LIDADFGEIE DPAKLHTDIK QLVGVVETGL FVQMAYKTYF
     GEESGEVKCW SK