RPIA_CANAL
ID RPIA_CANAL Reviewed; 240 AA.
AC Q5AJ92; A0A1D8PJ85;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Ribose-5-phosphate isomerase;
DE EC=5.3.1.6 {ECO:0000250|UniProtKB:P0A7Z0};
DE AltName: Full=D-ribose-5-phosphate ketol-isomerase;
DE AltName: Full=Phosphoriboisomerase;
GN Name=RKI1; OrderedLocusNames=CAALFM_C301480CA;
GN ORFNames=CaO19.1701, CaO19.9268;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- FUNCTION: Involved in the first step of the non-oxidative branch of the
CC pentose phosphate pathway. It catalyzes the reversible conversion of
CC ribose-5-phosphate to ribulose 5-phosphate.
CC {ECO:0000250|UniProtKB:P0A7Z0}.
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; Evidence={ECO:0000250|UniProtKB:P0A7Z0};
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribose
CC 5-phosphate from D-ribulose 5-phosphate (non-oxidative stage): step
CC 1/1. {ECO:0000250|UniProtKB:P0A7Z0}.
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; CP017625; AOW28190.1; -; Genomic_DNA.
DR RefSeq; XP_721773.2; XM_716680.2.
DR AlphaFoldDB; Q5AJ92; -.
DR SMR; Q5AJ92; -.
DR STRING; 237561.Q5AJ92; -.
DR PRIDE; Q5AJ92; -.
DR GeneID; 3636574; -.
DR KEGG; cal:CAALFM_C301480CA; -.
DR CGD; CAL0000188418; RKI1.
DR VEuPathDB; FungiDB:C3_01480C_A; -.
DR eggNOG; KOG3075; Eukaryota.
DR HOGENOM; CLU_056590_0_0_1; -.
DR InParanoid; Q5AJ92; -.
DR OMA; YDWDEVN; -.
DR OrthoDB; 1074761at2759; -.
DR UniPathway; UPA00115; UER00412.
DR PRO; PR:Q5AJ92; -.
DR Proteomes; UP000000559; Chromosome 3.
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..240
FT /note="Ribose-5-phosphate isomerase"
FT /id="PRO_0000339884"
FT ACT_SITE 110
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0A7Z0"
FT BINDING 34..37
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O50083"
FT BINDING 88..91
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O50083"
FT BINDING 101..104
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O50083"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O50083"
FT SITE 88
FT /note="Plays a direct or indirect catalytic role"
FT /evidence="ECO:0000250|UniProtKB:O50083"
SQ SEQUENCE 240 AA; 26003 MW; 12B7CACEF5FCD0A4 CRC64;
MSSTSKVESA KKLAAYKAVD ENFPKDAKVI GIGSGSTVIY AAERIGQLDN KDSFICIPTG
FQSKQLIIDN GLRLGTIEQY PDIDIAFDGA DEVDPQLNLI KGGGACLFQE KLVAASAKKF
VVVADYRKKS DKLGQSWRQG VPIEIVPNSY SKIIQELSKK LGAKNVDLRQ GGKAKAGPII
TDNNNFLLDA DFGEIEIDNV GKLHEQIKLL VGVVETGLFT NMANKAYFGE EDGSVSVWSK
