RPIA_YARLI
ID RPIA_YARLI Reviewed; 243 AA.
AC Q6CFH4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=YALI0B06941g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
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; CR382128; CAG82819.1; -; Genomic_DNA.
DR RefSeq; XP_500588.1; XM_500588.1.
DR AlphaFoldDB; Q6CFH4; -.
DR SMR; Q6CFH4; -.
DR STRING; 4952.CAG82819; -.
DR PRIDE; Q6CFH4; -.
DR EnsemblFungi; CAG82819; CAG82819; YALI0_B06941g.
DR GeneID; 2906709; -.
DR KEGG; yli:YALI0B06941g; -.
DR VEuPathDB; FungiDB:YALI0_B06941g; -.
DR HOGENOM; CLU_056590_0_0_1; -.
DR InParanoid; Q6CFH4; -.
DR OMA; YDWDEVN; -.
DR UniPathway; UPA00115; UER00412.
DR Proteomes; UP000001300; Chromosome B.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IBA:GO_Central.
DR GO; GO:0006014; P:D-ribose metabolic process; IBA:GO_Central.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
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..243
FT /note="Ribose-5-phosphate isomerase"
FT /id="PRO_0000339895"
SQ SEQUENCE 243 AA; 25954 MW; CC48A1EAA6306214 CRC64;
MSSELPPLEQ AKRIAAHQAV EQHYPKDAKV VGIGSGSTVV YVAEKIASLP KELTKDTVFI
STGFQSKQLI QNAGLRLGCI DQYSNGDLDV AFDGADETDP QLNCIKGGGA CLFQEKIVAE
CARKFVVVAD YRKQSKALGT VWIQGIPIEV VPDAYNKVIA DLKKMGAQSA VLRPGSPGKA
GPIITDNGNF IVDAYFGEIQ PDAVKDLHIK IKLLLGVVET GLFTNADVAY FGNADGTIST
ITK