CAPP2_ARATH
ID CAPP2_ARATH Reviewed; 963 AA.
AC Q5GM68; Q8GVE9; Q9SIN0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 25-MAY-2022, entry version 121.
DE RecName: Full=Phosphoenolpyruvate carboxylase 2;
DE Short=AtPPC2;
DE Short=PEPC 2;
DE Short=PEPCase 2;
DE EC=4.1.1.31;
GN Name=PPC2; OrderedLocusNames=At2g42600; ORFNames=F14N22.13;
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 [MRNA], TISSUE SPECIFICITY, AND NOMENCLATURE.
RC STRAIN=cv. Columbia;
RX PubMed=12805623; DOI=10.1104/pp.102.019653;
RA Sanchez R., Cejudo F.J.;
RT "Identification and expression analysis of a gene encoding a bacterial-type
RT phosphoenolpyruvate carboxylase from Arabidopsis and rice.";
RL Plant Physiol. 132:949-957(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zanor M.I., Plesch G., Mueller-Roeber B.;
RT "Cloning of Arabidopsis guard cell PEP carboxylase.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-701, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Root;
RX PubMed=18433157; DOI=10.1021/pr8000173;
RA de la Fuente van Bentem S., Anrather D., Dohnal I., Roitinger E.,
RA Csaszar E., Joore J., Buijnink J., Carreri A., Forzani C., Lorkovic Z.J.,
RA Barta A., Lecourieux D., Verhounig A., Jonak C., Hirt H.;
RT "Site-specific phosphorylation profiling of Arabidopsis proteins by mass
RT spectrometry and peptide chip analysis.";
RL J. Proteome Res. 7:2458-2470(2008).
CC -!- FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) it
CC forms oxaloacetate, a four-carbon dicarboxylic acid source for the
CC tricarboxylic acid cycle.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: By light-reversible phosphorylation.
CC {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in all plant organs, with higher levels
CC in stems and leaves. {ECO:0000269|PubMed:12805623}.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD22994.1; Type=Erroneous gene model prediction; Evidence={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; AJ532902; CAD58726.1; -; mRNA.
DR EMBL; AY210895; AAP43628.1; -; mRNA.
DR EMBL; AC007087; AAD22994.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC10145.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10146.1; -; Genomic_DNA.
DR EMBL; CP002685; ANM62337.1; -; Genomic_DNA.
DR PIR; H84855; H84855.
DR RefSeq; NP_001324501.1; NM_001336987.1.
DR RefSeq; NP_850372.4; NM_180041.5.
DR RefSeq; NP_850373.4; NM_180042.5.
DR AlphaFoldDB; Q5GM68; -.
DR SMR; Q5GM68; -.
DR BioGRID; 4197; 8.
DR STRING; 3702.AT2G42600.1; -.
DR iPTMnet; Q5GM68; -.
DR MetOSite; Q5GM68; -.
DR PaxDb; Q5GM68; -.
DR PRIDE; Q5GM68; -.
DR ProteomicsDB; 239093; -.
DR EnsemblPlants; AT2G42600.1; AT2G42600.1; AT2G42600.
DR EnsemblPlants; AT2G42600.2; AT2G42600.2; AT2G42600.
DR EnsemblPlants; AT2G42600.3; AT2G42600.3; AT2G42600.
DR GeneID; 818860; -.
DR Gramene; AT2G42600.1; AT2G42600.1; AT2G42600.
DR Gramene; AT2G42600.2; AT2G42600.2; AT2G42600.
DR Gramene; AT2G42600.3; AT2G42600.3; AT2G42600.
DR KEGG; ath:AT2G42600; -.
DR Araport; AT2G42600; -.
DR TAIR; locus:2041529; AT2G42600.
DR eggNOG; ENOG502QPVS; Eukaryota.
DR HOGENOM; CLU_006557_2_0_1; -.
DR InParanoid; Q5GM68; -.
DR OMA; PDYHVKV; -.
DR OrthoDB; 775417at2759; -.
DR PhylomeDB; Q5GM68; -.
DR BRENDA; 4.1.1.31; 399.
DR PRO; PR:Q5GM68; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q5GM68; baseline and differential.
DR Genevisible; Q5GM68; AT.
DR GO; GO:0048046; C:apoplast; HDA:TAIR.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IDA:TAIR.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR GO; GO:0048366; P:leaf development; IGI:TAIR.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR HAMAP; MF_00595; PEPcase_type1; 1.
DR InterPro; IPR021135; PEP_COase.
DR InterPro; IPR022805; PEP_COase_bac/pln-type.
DR InterPro; IPR018129; PEP_COase_Lys_AS.
DR InterPro; IPR033129; PEPCASE_His_AS.
DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR PANTHER; PTHR30523; PTHR30523; 1.
DR Pfam; PF00311; PEPcase; 1.
DR PRINTS; PR00150; PEPCARBXLASE.
DR SUPFAM; SSF51621; SSF51621; 1.
DR PROSITE; PS00781; PEPCASE_1; 1.
DR PROSITE; PS00393; PEPCASE_2; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Carbon dioxide fixation; Cytoplasm; Lyase; Magnesium;
KW Phosphoprotein; Photosynthesis; Reference proteome.
FT CHAIN 1..963
FT /note="Phosphoenolpyruvate carboxylase 2"
FT /id="PRO_0000166658"
FT ACT_SITE 172
FT /evidence="ECO:0000250"
FT ACT_SITE 599
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9MAH0"
FT MOD_RES 701
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18433157"
FT CONFLICT 453
FT /note="E -> D (in Ref. 2; AAP43628)"
FT /evidence="ECO:0000305"
FT CONFLICT 456
FT /note="S -> T (in Ref. 2; AAP43628)"
FT /evidence="ECO:0000305"
FT CONFLICT 770
FT /note="W -> R (in Ref. 1; CAD58726)"
FT /evidence="ECO:0000305"
FT CONFLICT 799
FT /note="S -> N (in Ref. 2; AAP43628)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 963 AA; 109753 MW; D2F000BC8087D845 CRC64;
MAARNLEKMA SIDAQLRLLA PGKVSEDDKL IEYDALLLDR FLDILQDLHG EDVREFVQEC
YEVAADYDGN RNTEKLEELG NMLTSLDPGD SIVVTKSFSN MLSLANLAEE VQIAYRRRIK
KLKKGDFADE ASATTESDIE ETLKRLLQLN KTPEEVFDAL KNQTVDLVLT AHPTQSVRRS
LLQKFGRIRD CLTQLYAKDI TPDDKQELDE ALQREIQAAF RTDEIRRTPP TPQDEMRAGM
SYFHETIWKG VPKFLRRVDT ALKNIGINER VPYNAPLIQF SSWMGGDRDG NPRVTPEVTR
DVCLLARMMA ANLYFSQIED LMFEMSMWRC NEELRVRAER QRCAKRDAKH YIEFWKQIPA
NEPYRAILGD VRDKLYNTRE RARQLLSSGV SDVPEDAVFT SVDQFLEPLE LCYRSLCDCG
DRPIADGSLL DFLRQVSTFG LALVKLDIRQ ESERHSDVLD AITTHLGIGS YKEWSEDKRQ
EWLLSELSGK RPLFGPDLPK TEEVADVLDT FKVISELPSD SFGAYIISMA TAPSDVLAVE
LLQRECGITD PLRVVPLFEK LADLESAPAA VARLFSIEWY RNRINGKQEV MIGYSDSGKD
AGRLSAAWQL YKTQEELVKV AKEYGVKLTM FHGRGGTVGR GGGPTHLAIL SQPPDTIHGQ
LRVTVQGEVI EQSFGEEHLC FRTLQRFTAA TLEHGMHPPV SPKPEWRVLM DEMAIIATEE
YRSVVFKEPR FVEYFRLATP ELEYGRMNIG SRPSKRKPSG GIESLRAIPW IFAWTQTRFH
LPVWLGFGGA FKRVIQKDSK NLNMLKEMYN QWPFFRVTID LVEMVFAKGD PGIAALYDRL
LVSEELQPFG EQLRVNYQET RRLLLQVAGH KDILEGDPYL RQRLQLRDPY ITTLNVCQAY
TLKQIRDPSF HVKVRPHLSK DYMESSPAAE LVKLNPKSEY APGLEDTVIL TMKGIAAGMQ
NTG
