RPI1_ARATH
ID RPI1_ARATH Reviewed; 267 AA.
AC Q9C998; Q8LBQ2; Q9C5D1;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Probable ribose-5-phosphate isomerase 1;
DE EC=5.3.1.6;
DE AltName: Full=Phosphoriboisomerase 1;
DE AltName: Full=Protein RADIAL SWELLING 10;
GN Name=RPI1; Synonyms=RSW10; OrderedLocusNames=At1g71100; ORFNames=F23N20.9;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(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 TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-115.
RX PubMed=17059404; DOI=10.1111/j.1365-313x.2006.02902.x;
RA Howles P.A., Birch R.J., Collings D.A., Gebbie L.K., Hurley U.A.,
RA Hocart C.H., Arioli T., Williamson R.E.;
RT "A mutation in an Arabidopsis ribose 5-phosphate isomerase reduces
RT cellulose synthesis and is rescued by exogenous uridine.";
RL Plant J. 48:606-618(2006).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT GLY-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: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: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, cotyledons, leaves and flowers.
CC {ECO:0000269|PubMed:17059404}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions (permissive temperature of 21 degrees Celsius), but mutant
CC plants have a temperature-sensitive phenotype (when transferred to 31
CC degrees Celsius) showing radially swollen roots and reduction in
CC cellulose production. {ECO:0000269|PubMed:17059404}.
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; AC016972; AAG51684.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE35161.1; -; Genomic_DNA.
DR EMBL; AF360330; AAK26040.1; -; mRNA.
DR EMBL; AY142637; AAN13095.1; -; mRNA.
DR EMBL; AY087060; AAM64621.1; -; mRNA.
DR PIR; E96735; E96735.
DR RefSeq; NP_177266.1; NM_105779.4.
DR AlphaFoldDB; Q9C998; -.
DR SMR; Q9C998; -.
DR STRING; 3702.AT1G71100.1; -.
DR iPTMnet; Q9C998; -.
DR PaxDb; Q9C998; -.
DR PRIDE; Q9C998; -.
DR ProteomicsDB; 228230; -.
DR EnsemblPlants; AT1G71100.1; AT1G71100.1; AT1G71100.
DR GeneID; 843450; -.
DR Gramene; AT1G71100.1; AT1G71100.1; AT1G71100.
DR KEGG; ath:AT1G71100; -.
DR Araport; AT1G71100; -.
DR TAIR; locus:2026296; AT1G71100.
DR eggNOG; KOG3075; Eukaryota.
DR HOGENOM; CLU_056590_1_2_1; -.
DR InParanoid; Q9C998; -.
DR OMA; GHYIVDL; -.
DR OrthoDB; 1074761at2759; -.
DR PhylomeDB; Q9C998; -.
DR BioCyc; ARA:AT1G71100-MON; -.
DR UniPathway; UPA00115; UER00412.
DR PRO; PR:Q9C998; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C998; baseline and differential.
DR Genevisible; Q9C998; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0030244; P:cellulose biosynthetic process; IMP:TAIR.
DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IEA:InterPro.
DR GO; GO:0046109; P:uridine biosynthetic process; 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..267
FT /note="Probable ribose-5-phosphate isomerase 1"
FT /id="PRO_0000425979"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9S726"
FT MUTAGEN 115
FT /note="E->K: In rsw10; temperature-sensitive radial
FT swelling of roots and reduction in cellulose production."
FT /evidence="ECO:0000269|PubMed:17059404"
FT CONFLICT 211
FT /note="R -> G (in Ref. 4; AAM64621)"
FT /evidence="ECO:0000305"
FT CONFLICT 241
FT /note="E -> K (in Ref. 3; AAK26040)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 28332 MW; B8E32287BF2DE8E3 CRC64;
MGSAFDPLVT ATEDLAAVNS APPLSNLTQE ELKKIAAYKA VEFVESGMVI GLGTGSTAKH
AVARISELLR EGKLKDIIGI PTSTTTHEQA VSLGIPLSDL DSHPVVDLSI DGADEVDPAL
NLVKGRGGSL LREKMIEGAS KKFVVIVDES KLVKYIGGSG LAVPVEVVPF CCDFTRGKLE
ELFRDSGCVA KLRMKIGSNG EEAAPAVTDN RNYVVDLYLE RDIGDLEVAS EAILRFPGVV
EHGMFLGMAT TLIVAGKFGV TVKDRFG