RPI2_ARATH
ID RPI2_ARATH Reviewed; 265 AA.
AC Q9ZU38; Q1PFB3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Probable ribose-5-phosphate isomerase 2;
DE EC=5.3.1.6;
DE AltName: Full=Phosphoriboisomerase 2;
GN Name=RPI2; OrderedLocusNames=At2g01290; ORFNames=F10A8.17;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=17147637; DOI=10.1111/j.1467-7652.2006.00183.x;
RA Underwood B.A., Vanderhaeghen R., Whitford R., Town C.D., Hilson P.;
RT "Simultaneous high-throughput recombinational cloning of open reading
RT frames in closed and open configurations.";
RL Plant Biotechnol. J. 4:317-324(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19744161; DOI=10.1111/j.1399-3054.2009.01276.x;
RA Xiong Y., DeFraia C., Williams D., Zhang X., Mou Z.;
RT "Deficiency in a cytosolic ribose-5-phosphate isomerase causes chloroplast
RT dysfunction, late flowering and premature cell death in Arabidopsis.";
RL Physiol. Plantarum 137:249-263(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Catalyzes the reversible conversion of ribose-5-phosphate to
CC ribulose 5-phosphate. {ECO:0000269|PubMed:19744161}.
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:0000269|PubMed:19744161};
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:0000269|PubMed:19744161}.
CC -!- DISRUPTION PHENOTYPE: Retarded growth and slight chlorosis due to
CC decreased chloroplast photosynthetic capacity. Reduced accumulation of
CC starch in leaves. Late flowering when grown under short-day conditions.
CC {ECO:0000269|PubMed:19744161}.
CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC {ECO:0000305}.
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DR EMBL; AC006200; AAD14529.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC05429.1; -; Genomic_DNA.
DR EMBL; DQ446450; ABE65420.1; -; Genomic_DNA.
DR EMBL; AY054172; AAL06833.1; -; mRNA.
DR EMBL; AY066038; AAL47405.1; -; mRNA.
DR PIR; H84422; H84422.
DR RefSeq; NP_178238.1; NM_126190.1.
DR AlphaFoldDB; Q9ZU38; -.
DR SMR; Q9ZU38; -.
DR BioGRID; 61; 2.
DR IntAct; Q9ZU38; 1.
DR STRING; 3702.AT2G01290.1; -.
DR iPTMnet; Q9ZU38; -.
DR PaxDb; Q9ZU38; -.
DR PRIDE; Q9ZU38; -.
DR ProteomicsDB; 226918; -.
DR EnsemblPlants; AT2G01290.1; AT2G01290.1; AT2G01290.
DR GeneID; 814657; -.
DR Gramene; AT2G01290.1; AT2G01290.1; AT2G01290.
DR KEGG; ath:AT2G01290; -.
DR Araport; AT2G01290; -.
DR TAIR; locus:2038801; AT2G01290.
DR eggNOG; KOG3075; Eukaryota.
DR HOGENOM; CLU_056590_1_2_1; -.
DR InParanoid; Q9ZU38; -.
DR OMA; GCEANLR; -.
DR OrthoDB; 1074761at2759; -.
DR PhylomeDB; Q9ZU38; -.
DR BioCyc; ARA:AT2G01290-MON; -.
DR BRENDA; 5.3.1.6; 399.
DR UniPathway; UPA00115; UER00412.
DR PRO; PR:Q9ZU38; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZU38; baseline and differential.
DR Genevisible; Q9ZU38; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IDA:TAIR.
DR GO; GO:0008219; P:cell death; IMP:TAIR.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:InterPro.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IMP:TAIR.
DR CDD; cd01398; RPI_A; 1.
DR HAMAP; MF_00170; Rib_5P_isom_A; 1.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR InterPro; IPR020672; Ribose5P_isomerase_typA_subgr.
DR InterPro; IPR004788; Ribose5P_isomerase_type_A.
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 Acetylation; Cytoplasm; Isomerase; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..265
FT /note="Probable ribose-5-phosphate isomerase 2"
FT /id="PRO_0000158525"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 96
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9S726"
SQ SEQUENCE 265 AA; 28516 MW; 4A6587E6543691C1 CRC64;
MALAYDPLFI TSDKSLSAFD VASSPPQPMN LTQDELKRIA AYKAVEFVES GMVLGLGTGS
TAKHAVDRIG ELLRQGKLEN IVGIPTSKKT QEQALSLGIP LSDLDAHPVI DLSIDGADEV
DPFLNLVKGR GGSLLREKMI EGASKKFVVI VDDSKMVKHI GGSKLALPVE IVPFCWKFTA
EKLRSLLEGY GCEANLRLGE KGKAFVTDNG NYIVDMHVEE DMGDLGAVSD AILRLPGVVE
HGMFLDMAST VIIAGELGVK IKNKH
