CA1P_ARATH
ID CA1P_ARATH Reviewed; 482 AA.
AC Q9FNJ9;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Probable 2-carboxy-D-arabinitol-1-phosphatase {ECO:0000305};
DE EC=3.1.3.63 {ECO:0000250|UniProtKB:W5EP13};
DE Flags: Precursor;
GN OrderedLocusNames=At5g22620 {ECO:0000312|Araport:AT5G22620};
GN ORFNames=MDJ22.4 {ECO:0000312|EMBL:BAB11668.1};
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=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
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 IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21365755; DOI=10.1002/pmic.201000495;
RA Bayer R.G., Stael S., Csaszar E., Teige M.;
RT "Mining the soluble chloroplast proteome by affinity chromatography.";
RL Proteomics 11:1287-1299(2011).
CC -!- FUNCTION: Phosphoglycerate mutase-like protein lacking PGM activity,
CC but having 2-carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase
CC activity. Prevents the accumulation of D-glycero-2,3-pentodiulose-1,5-
CC bisphosphate (PDBP) a potent inhibitor of ribulose-1,5-bisphosphate
CC carboxylase (RuBisCO). PDBP is produced during the oxidation of
CC ribulose-1,5-bisphosphate, the substrate of RuBisCO.
CC {ECO:0000250|UniProtKB:W5EP13}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-carboxy-D-arabinitol 1-phosphate + H2O = 2-carboxy-D-
CC arabinitol + phosphate; Xref=Rhea:RHEA:17837, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58008, ChEBI:CHEBI:58185; EC=3.1.3.63;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000269|PubMed:21365755}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9FNJ9-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC {ECO:0000305}.
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DR EMBL; AB006699; BAB11668.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93052.1; -; Genomic_DNA.
DR EMBL; CP002688; AED93053.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM68791.1; -; Genomic_DNA.
DR EMBL; AY062480; AAL32558.1; -; mRNA.
DR EMBL; AY093258; AAM13257.1; -; mRNA.
DR RefSeq; NP_001154730.1; NM_001161258.1. [Q9FNJ9-1]
DR RefSeq; NP_001330513.1; NM_001343744.1. [Q9FNJ9-1]
DR RefSeq; NP_197654.1; NM_122168.5. [Q9FNJ9-1]
DR AlphaFoldDB; Q9FNJ9; -.
DR SMR; Q9FNJ9; -.
DR BioGRID; 17600; 1.
DR IntAct; Q9FNJ9; 1.
DR STRING; 3702.AT5G22620.1; -.
DR PaxDb; Q9FNJ9; -.
DR PRIDE; Q9FNJ9; -.
DR ProteomicsDB; 240310; -. [Q9FNJ9-1]
DR EnsemblPlants; AT5G22620.1; AT5G22620.1; AT5G22620. [Q9FNJ9-1]
DR EnsemblPlants; AT5G22620.2; AT5G22620.2; AT5G22620. [Q9FNJ9-1]
DR EnsemblPlants; AT5G22620.5; AT5G22620.5; AT5G22620. [Q9FNJ9-1]
DR GeneID; 832325; -.
DR Gramene; AT5G22620.1; AT5G22620.1; AT5G22620. [Q9FNJ9-1]
DR Gramene; AT5G22620.2; AT5G22620.2; AT5G22620. [Q9FNJ9-1]
DR Gramene; AT5G22620.5; AT5G22620.5; AT5G22620. [Q9FNJ9-1]
DR KEGG; ath:AT5G22620; -.
DR Araport; AT5G22620; -.
DR TAIR; locus:2162449; AT5G22620.
DR eggNOG; KOG0235; Eukaryota.
DR InParanoid; Q9FNJ9; -.
DR OMA; VQMPEGE; -.
DR OrthoDB; 1112626at2759; -.
DR PhylomeDB; Q9FNJ9; -.
DR PRO; PR:Q9FNJ9; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FNJ9; baseline and differential.
DR Genevisible; Q9FNJ9; AT.
DR GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0047538; F:2-carboxy-D-arabinitol-1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; -; 2.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR Pfam; PF00300; His_Phos_1; 2.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; SSF53254; 2.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Hydrolase; Plastid; Reference proteome;
KW Transit peptide.
FT TRANSIT 1..34
FT /note="Chloroplast"
FT /evidence="ECO:0000305"
FT CHAIN 35..482
FT /note="Probable 2-carboxy-D-arabinitol-1-phosphatase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000430637"
FT ACT_SITE 55
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P62707"
FT ACT_SITE 129
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P62707"
SQ SEQUENCE 482 AA; 53114 MW; 3EA8C450B12D2B51 CRC64;
MISLPLTTPI LPSRCLLHKT RRQNSTRRRL LIRSSSSLQD QFTVETTKRV VLVRHGQSTW
NEEGRIQGSS DFSVLTKKGE SQAEISRQML IDDSFDVCFT SPLKRSKKTA EIIWGSRESE
MIFDYDLREI DLYSFQGLLK KEGKEKFGEA FKQWQEDPAN FIIDGHYPVR ELWSRARSCW
PGILAHESKS VLVVAHNAVN QALLATAIGL GTEYFRSLLQ SNCGVSVLDF IPRADGGSPH
VCLNRLNQTP NSPLAGGSSG GRKASKQIIL VCHGQGNNED SAVINQAANN DQAMNMLGVI
HSQKTAELLL DLRVSSIVCS PKTASIESSG VISRVQEAAG CLGVDNVPHY VKTKQMNELD
VESVLRKSNK DNDVIASQLD EEAFSALWNR SEKAWESLLD ELSDEKSNPG EIMVVVGPAM
THISLIAQCL NLTKEALGLF HLDAGSISVI DFPDGPSSKG VIRCTNYTAH LGRWSIPITK
PA
