CA1P_WHEAT
ID CA1P_WHEAT Reviewed; 495 AA.
AC W5EP13; G4VUY9;
DT 29-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=2-carboxy-D-arabinitol-1-phosphatase {ECO:0000305};
DE EC=3.1.3.63 {ECO:0000269|PubMed:22132794};
DE Flags: Precursor;
OS Triticum aestivum (Wheat).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX NCBI_TaxID=4565;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Chinese Spring;
RX PubMed=23192148; DOI=10.1038/nature11650;
RA Brenchley R., Spannagl M., Pfeifer M., Barker G.L., D'Amore R., Allen A.M.,
RA McKenzie N., Kramer M., Kerhornou A., Bolser D., Kay S., Waite D.,
RA Trick M., Bancroft I., Gu Y., Huo N., Luo M.C., Sehgal S., Gill B.,
RA Kianian S., Anderson O., Kersey P., Dvorak J., McCombie W.R., Hall A.,
RA Mayer K.F., Edwards K.J., Bevan M.W., Hall N.;
RT "Analysis of the bread wheat genome using whole-genome shotgun
RT sequencing.";
RL Nature 491:705-710(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 51-495, FUNCTION, CATALYTIC ACTIVITY,
RP ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22132794; DOI=10.1042/bj20111443;
RA Andralojc P.J., Madgwick P.J., Tao Y., Keys A., Ward J.L., Beale M.H.,
RA Loveland J.E., Jackson P.J., Willis A.C., Gutteridge S., Parry M.A.;
RT "2-Carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase: evidence for a
RT wider role in plant Rubisco regulation.";
RL Biochem. J. 442:733-742(2012).
CC -!- FUNCTION: Phosphoglycerate mutase-like protein lacking PGM activity,
CC but having 2-carboxy-D-arabinitol 1-phosphate (CA1P) phosphatase
CC activity. Can dephosphorylate the closely related compounds 2-carboxy-
CC D-arabinitol 1,5-bisphosphate (CABP) and 2-carboxy-D-ribitol-1,5-
CC bisphosphate(CRBP), and 2,3-diphosphoglycerate. Prevents the
CC accumulation of D-glycero-2,3-pentodiulose-1,5-bisphosphate (PDBP) a
CC potent inhibitor of ribulose-1,5-bisphosphate carboxylase (RuBisCO).
CC PDBP is produced during the oxidation of ribulose-1,5-bisphosphate, the
CC substrate of RuBisCO. {ECO:0000269|PubMed:22132794}.
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 Evidence={ECO:0000269|PubMed:22132794};
CC -!- ACTIVITY REGULATION: Inactivated by oxidized glutathione (GSSG) at pH
CC 8.0. {ECO:0000269|PubMed:22132794}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for 2-carboxy-D-arabinitol 1-phosphate
CC {ECO:0000269|PubMed:22132794};
CC KM=2.9 uM for 2-carboxy-D-arabinitol 1,5-bisphosphate
CC {ECO:0000269|PubMed:22132794};
CC KM=4.3 uM for 2-carboxy-D-ribitol-1,5-bisphosphate
CC {ECO:0000269|PubMed:22132794};
CC KM=184 uM for 2,3-diphosphoglycerate {ECO:0000269|PubMed:22132794};
CC Vmax=4.2 umol/min/mg enzyme toward 2-carboxy-D-arabinitol 1-phosphate
CC {ECO:0000269|PubMed:22132794};
CC Vmax=4.3 umol/min/mg enzyme toward 2-carboxy-D-arabinitol 1,5-
CC bisphosphate {ECO:0000269|PubMed:22132794};
CC Vmax=3.9 umol/min/mg enzyme toward 2-carboxy-D-ribitol 1,5-
CC bisphosphate {ECO:0000269|PubMed:22132794};
CC Vmax=6.1 umol/min/mg enzyme toward 2,3-diphosphoglycerate
CC {ECO:0000269|PubMed:22132794};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:22132794};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast stroma
CC {ECO:0000250|UniProtKB:Q9FNJ9}.
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family.
CC {ECO:0000305}.
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DR EMBL; HE603918; CCE25835.1; -; mRNA.
DR AlphaFoldDB; W5EP13; -.
DR SMR; W5EP13; -.
DR STRING; 4565.Traes_4DS_1860220B9.1; -.
DR PRIDE; W5EP13; -.
DR EnsemblPlants; TraesCAD_scaffold_100849_01G000200.1; TraesCAD_scaffold_100849_01G000200.1; TraesCAD_scaffold_100849_01G000200.
DR EnsemblPlants; TraesCLE_scaffold_094133_01G000200.1; TraesCLE_scaffold_094133_01G000200.1; TraesCLE_scaffold_094133_01G000200.
DR EnsemblPlants; TraesCS4D02G129300.1; TraesCS4D02G129300.1; TraesCS4D02G129300.
DR EnsemblPlants; TraesPAR_scaffold_103188_01G000300.1; TraesPAR_scaffold_103188_01G000300.1; TraesPAR_scaffold_103188_01G000300.
DR EnsemblPlants; TraesROB_scaffold_002225_01G000300.1; TraesROB_scaffold_002225_01G000300.1; TraesROB_scaffold_002225_01G000300.
DR EnsemblPlants; TraesWEE_scaffold_081482_01G000300.1; TraesWEE_scaffold_081482_01G000300.1; TraesWEE_scaffold_081482_01G000300.
DR Gramene; TraesCAD_scaffold_100849_01G000200.1; TraesCAD_scaffold_100849_01G000200.1; TraesCAD_scaffold_100849_01G000200.
DR Gramene; TraesCLE_scaffold_094133_01G000200.1; TraesCLE_scaffold_094133_01G000200.1; TraesCLE_scaffold_094133_01G000200.
DR Gramene; TraesCS4D02G129300.1; TraesCS4D02G129300.1; TraesCS4D02G129300.
DR Gramene; TraesPAR_scaffold_103188_01G000300.1; TraesPAR_scaffold_103188_01G000300.1; TraesPAR_scaffold_103188_01G000300.
DR Gramene; TraesROB_scaffold_002225_01G000300.1; TraesROB_scaffold_002225_01G000300.1; TraesROB_scaffold_002225_01G000300.
DR Gramene; TraesWEE_scaffold_081482_01G000300.1; TraesWEE_scaffold_081482_01G000300.1; TraesWEE_scaffold_081482_01G000300.
DR eggNOG; KOG0235; Eukaryota.
DR HOGENOM; CLU_035286_0_0_1; -.
DR OMA; PRICLNR; -.
DR Proteomes; UP000019116; Unplaced.
DR ExpressionAtlas; W5EP13; baseline and differential.
DR Genevisible; W5EP13; TA.
DR GO; GO:0009570; C:chloroplast stroma; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0047538; F:2-carboxy-D-arabinitol-1-phosphatase activity; IDA:UniProtKB.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0016311; P:dephosphorylation; IDA:UniProtKB.
DR CDD; cd07067; HP_PGM_like; 2.
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; 2.
DR SUPFAM; SSF53254; SSF53254; 2.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Hydrolase; Plastid; Reference proteome; Transit peptide.
FT TRANSIT 1..50
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 51..495
FT /note="2-carboxy-D-arabinitol-1-phosphatase"
FT /evidence="ECO:0000255"
FT /id="PRO_0000430638"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 58
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P62707"
FT ACT_SITE 132
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P62707"
SQ SEQUENCE 495 AA; 53825 MW; EC7D659257B57DDF CRC64;
MLLFAPTPPP SPATAHRRPG GSAASCIRCS SVRELDRSPS RPPLPPLAEA KRVVLVRHGQ
STWNADGRIQ GSSDFSVLTP KGESQAETSR LMLLADSFDA CFTSPLARSR RTAEIIWDTR
DKDLIPDYDL REIDLYSFQG LLKHEGKEKY GALFQQWQKN PSDCSIDGHY PVRELWDRAQ
GCWERILTHE GKSVLVVAHN AVNQALVATS LGLGTEYFRT LLQSNCGASV LDFTPQPGGR
PPSVCLNRLN QTPSSPISAE SSAGRKSSKR IILVCQGATQ SSSEGSLGGV GYAPLNMLGV
IQAQKTAELL LDLKVNSIIC SPQVAAVDTA TAICEVQEAA GCLGADCVPR YVEMKNLLGL
EIDDAFLTKQ KSLEQIVQSG WMGGMEHQKL KTLWAQSEDA WQALVNELPE DDGAESDRVV
VAIGHPAIHL GLLCRCLNLT MDYMPSFHLD DGSISVIDFP DGPKGGGIVR CTNYTAHLGR
WSVPITKSTE NNDEF
