RPIA_YEAST
ID RPIA_YEAST Reviewed; 258 AA.
AC Q12189; D6W2F6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Ribose-5-phosphate isomerase {ECO:0000303|PubMed:8929392};
DE EC=5.3.1.6 {ECO:0000305|PubMed:8929392};
DE AltName: Full=D-ribose-5-phosphate ketol-isomerase;
DE AltName: Full=Phosphoriboisomerase;
GN Name=RKI1; OrderedLocusNames=YOR095C; ORFNames=YOR3174C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9200815;
RX DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA Schwager C., Paces V., Sander C., Ansorge W.;
RT "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL Yeast 13:655-672(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP CHARACTERIZATION, AND CATALYTIC ACTIVITY.
RX PubMed=8929392; DOI=10.1007/s002940050149;
RA Miosga T., Zimmermann F.K.;
RT "Cloning and characterization of the first two genes of the non-oxidative
RT part of the Saccharomyces cerevisiae pentose-phosphate pathway.";
RL Curr. Genet. 30:404-409(1996).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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:0000305|PubMed:8929392};
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 -!- MISCELLANEOUS: Present with 5680 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X94335; CAA64017.1; -; Genomic_DNA.
DR EMBL; Z75003; CAA99292.1; -; Genomic_DNA.
DR EMBL; BK006948; DAA10872.1; -; Genomic_DNA.
DR PIR; S61656; S61656.
DR RefSeq; NP_014738.1; NM_001183514.1.
DR PDB; 1XTZ; X-ray; 2.10 A; A=1-258.
DR PDBsum; 1XTZ; -.
DR AlphaFoldDB; Q12189; -.
DR SMR; Q12189; -.
DR BioGRID; 34493; 102.
DR DIP; DIP-4155N; -.
DR IntAct; Q12189; 8.
DR MINT; Q12189; -.
DR STRING; 4932.YOR095C; -.
DR iPTMnet; Q12189; -.
DR MaxQB; Q12189; -.
DR PaxDb; Q12189; -.
DR PRIDE; Q12189; -.
DR EnsemblFungi; YOR095C_mRNA; YOR095C; YOR095C.
DR GeneID; 854262; -.
DR KEGG; sce:YOR095C; -.
DR SGD; S000005621; RKI1.
DR VEuPathDB; FungiDB:YOR095C; -.
DR eggNOG; KOG3075; Eukaryota.
DR GeneTree; ENSGT00390000004352; -.
DR HOGENOM; CLU_056590_0_0_1; -.
DR InParanoid; Q12189; -.
DR OMA; YDWDEVN; -.
DR BioCyc; YEAST:YOR095C-MON; -.
DR Reactome; R-SCE-71336; Pentose phosphate pathway.
DR SABIO-RK; Q12189; -.
DR UniPathway; UPA00115; UER00412.
DR EvolutionaryTrace; Q12189; -.
DR PRO; PR:Q12189; -.
DR Proteomes; UP000002311; Chromosome XV.
DR RNAct; Q12189; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IMP:SGD.
DR GO; GO:0006014; P:D-ribose metabolic process; IBA:GO_Central.
DR GO; GO:0006098; P:pentose-phosphate shunt; IMP:SGD.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central.
DR GO; GO:0008615; P:pyridoxine biosynthetic process; IMP:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Isomerase; Reference proteome.
FT CHAIN 1..258
FT /note="Ribose-5-phosphate isomerase"
FT /id="PRO_0000158524"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:1XTZ"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:1XTZ"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1XTZ"
FT HELIX 51..61
FT /evidence="ECO:0007829|PDB:1XTZ"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:1XTZ"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:1XTZ"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:1XTZ"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:1XTZ"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:1XTZ"
FT STRAND 101..107
FT /evidence="ECO:0007829|PDB:1XTZ"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1XTZ"
FT HELIX 126..133
FT /evidence="ECO:0007829|PDB:1XTZ"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:1XTZ"
FT HELIX 145..147
FT /evidence="ECO:0007829|PDB:1XTZ"
FT STRAND 150..153
FT /evidence="ECO:0007829|PDB:1XTZ"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:1XTZ"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:1XTZ"
FT HELIX 170..179
FT /evidence="ECO:0007829|PDB:1XTZ"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:1XTZ"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:1XTZ"
FT STRAND 195..198
FT /evidence="ECO:0007829|PDB:1XTZ"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:1XTZ"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:1XTZ"
FT HELIX 218..226
FT /evidence="ECO:0007829|PDB:1XTZ"
FT STRAND 231..237
FT /evidence="ECO:0007829|PDB:1XTZ"
FT STRAND 242..247
FT /evidence="ECO:0007829|PDB:1XTZ"
FT STRAND 253..258
FT /evidence="ECO:0007829|PDB:1XTZ"
SQ SEQUENCE 258 AA; 28258 MW; E9F72BF2759F4DDD CRC64;
MAAGVPKIDA LESLGNPLED AKRAAAYRAV DENLKFDDHK IIGIGSGSTV VYVAERIGQY
LHDPKFYEVA SKFICIPTGF QSRNLILDNK LQLGSIEQYP RIDIAFDGAD EVDENLQLIK
GGGACLFQEK LVSTSAKTFI VVADSRKKSP KHLGKNWRQG VPIEIVPSSY VRVKNDLLEQ
LHAEKVDIRQ GGSAKAGPVV TDNNNFIIDA DFGEISDPRK LHREIKLLVG VVETGLFIDN
ASKAYFGNSD GSVEVTEK
