RPI3_ARATH
ID RPI3_ARATH Reviewed; 276 AA.
AC Q9S726; Q8L9K5;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Probable ribose-5-phosphate isomerase 3, chloroplastic;
DE EC=5.3.1.6;
DE AltName: Full=Phosphoriboisomerase 3;
DE AltName: Full=Protein EMBRYO DEFECTIVE 3119;
DE Flags: Precursor;
GN Name=RPI3; Synonyms=EMB3119; OrderedLocusNames=At3g04790;
GN ORFNames=F7O18.28, T9J14.26;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PHOSPHORYLATION.
RX PubMed=17404219; DOI=10.1073/pnas.0610208104;
RA Shin R., Alvarez S., Burch A.Y., Jez J.M., Schachtman D.P.;
RT "Phosphoproteomic identification of targets of the Arabidopsis sucrose
RT nonfermenting-like kinase SnRK2.8 reveals a connection to metabolic
RT processes.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:6460-6465(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-108, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22092075; DOI=10.1021/pr200917t;
RA Aryal U.K., Krochko J.E., Ross A.R.;
RT "Identification of phosphoproteins in Arabidopsis thaliana leaves using
RT polyethylene glycol fractionation, immobilized metal-ion affinity
RT chromatography, two-dimensional gel electrophoresis and mass
RT spectrometry.";
RL J. Proteome Res. 11:425-437(2012).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-40, CLEAVAGE OF TRANSIT PEPTIDE
RP [LARGE SCALE ANALYSIS] AFTER GLN-39, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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:0000250}.
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: Plastid, chloroplast {ECO:0000305}.
CC -!- PTM: Phosphorylated by SRK2C. {ECO:0000269|PubMed:17404219}.
CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family.
CC {ECO:0000305}.
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DR EMBL; AC009465; AAG51427.1; -; Genomic_DNA.
DR EMBL; AC011437; AAF04905.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74136.1; -; Genomic_DNA.
DR EMBL; AY045785; AAK76459.1; -; mRNA.
DR EMBL; AY142600; AAN13169.1; -; mRNA.
DR EMBL; AY088382; AAM65920.1; -; mRNA.
DR RefSeq; NP_187130.1; NM_111351.4.
DR AlphaFoldDB; Q9S726; -.
DR SMR; Q9S726; -.
DR BioGRID; 4974; 2.
DR IntAct; Q9S726; 2.
DR MINT; Q9S726; -.
DR STRING; 3702.AT3G04790.1; -.
DR iPTMnet; Q9S726; -.
DR MetOSite; Q9S726; -.
DR PaxDb; Q9S726; -.
DR PRIDE; Q9S726; -.
DR ProMEX; Q9S726; -.
DR ProteomicsDB; 227955; -.
DR EnsemblPlants; AT3G04790.1; AT3G04790.1; AT3G04790.
DR GeneID; 819639; -.
DR Gramene; AT3G04790.1; AT3G04790.1; AT3G04790.
DR KEGG; ath:AT3G04790; -.
DR Araport; AT3G04790; -.
DR TAIR; locus:2084898; AT3G04790.
DR eggNOG; KOG3075; Eukaryota.
DR HOGENOM; CLU_056590_1_2_1; -.
DR InParanoid; Q9S726; -.
DR OMA; YDWDEVN; -.
DR OrthoDB; 1074761at2759; -.
DR PhylomeDB; Q9S726; -.
DR BioCyc; ARA:AT3G04790-MON; -.
DR UniPathway; UPA00115; UER00412.
DR PRO; PR:Q9S726; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9S726; baseline and differential.
DR Genevisible; Q9S726; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009535; C:chloroplast thylakoid membrane; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009579; C:thylakoid; HDA:TAIR.
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 GO; GO:0019253; P:reductive pentose-phosphate cycle; NAS: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; Chloroplast; Isomerase; Phosphoprotein; Plastid;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..39
FT /note="Chloroplast"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 40..276
FT /note="Probable ribose-5-phosphate isomerase 3,
FT chloroplastic"
FT /id="PRO_0000425980"
FT MOD_RES 40
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22092075"
FT CONFLICT 197
FT /note="D -> E (in Ref. 4; AAM65920)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 276 AA; 29306 MW; E32D7000DA45722A CRC64;
MASLSFVSSS HLTLRTPSIA LRSTGSSPRT SVSFSVKAQS VALSQDDLKK LAAEKAVEAI
KPGMVLGLGT GSTAAFAVDQ IGKLLSSGEL YDIVGIPTSK RTEEQARSLG IPLVGLDTHP
RIDLAIDGAD EVDPNLDLVK GRGGALLREK MVEAVADKFI VVADDTKLVT GLGGSGLAMP
VEVVQFCWNF NLIRLQDLFK EFGCESKLRV DGDGKPYVTD NSNYIIDLYF KTPLKDGFAA
AKEIGKFQGV VEHGLFLGMA TSVIIAGKNG VEVMTK
