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Database: UniProt/SWISS-PROT
Entry: CAPP2_ARATH
LinkDB: CAPP2_ARATH
Original site: 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   22-NOV-2017, entry version 101.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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
RT   bacterial-type phosphoenolpyruvate carboxylase from Arabidopsis and
RT   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.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-701, AND IDENTIFICATION
RP   BY 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.,
RA   Lorkovic Z.J., Barta A., Lecourieux D., Verhounig A., Jonak C.,
RA   Hirt H.;
RT   "Site-specific phosphorylation profiling of Arabidopsis proteins by
RT   mass spectrometry and peptide chip analysis.";
RL   J. Proteome Res. 7:2458-2470(2008).
CC   -!- FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP)
CC       it forms oxaloacetate, a four-carbon dicarboxylic acid source for
CC       the tricarboxylic acid cycle.
CC   -!- CATALYTIC ACTIVITY: Phosphate + oxaloacetate = H(2)O +
CC       phosphoenolpyruvate + HCO(3)(-).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ENZYME 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
CC       levels 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};
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   UniGene; At.14366; -.
DR   ProteinModelPortal; Q5GM68; -.
DR   SMR; Q5GM68; -.
DR   BioGrid; 4197; 2.
DR   STRING; 3702.AT2G42600.1; -.
DR   iPTMnet; Q5GM68; -.
DR   PaxDb; Q5GM68; -.
DR   PRIDE; Q5GM68; -.
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; ENOG410IEAR; Eukaryota.
DR   eggNOG; COG2352; LUCA.
DR   HOGENOM; HOG000238648; -.
DR   InParanoid; Q5GM68; -.
DR   KO; K01595; -.
DR   OMA; GPTHRFI; -.
DR   OrthoDB; EOG0936013M; -.
DR   PhylomeDB; Q5GM68; -.
DR   BioCyc; ARA:GQT-2357-MONOMER; -.
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; IDA:TAIR.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0005829; C:cytosol; IDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; IDA: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; Complete proteome;
KW   Cytoplasm; Lyase; Magnesium; Phosphoprotein; Photosynthesis;
KW   Reference proteome.
FT   CHAIN         1    963       Phosphoenolpyruvate carboxylase 2.
FT                                /FTId=PRO_0000166658.
FT   ACT_SITE    172    172       {ECO:0000250}.
FT   ACT_SITE    599    599       {ECO:0000250}.
FT   MOD_RES      11     11       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q9MAH0}.
FT   MOD_RES     701    701       Phosphoserine.
FT                                {ECO:0000244|PubMed:18433157}.
FT   CONFLICT    453    453       E -> D (in Ref. 2; AAP43628).
FT                                {ECO:0000305}.
FT   CONFLICT    456    456       S -> T (in Ref. 2; AAP43628).
FT                                {ECO:0000305}.
FT   CONFLICT    770    770       W -> R (in Ref. 1; CAD58726).
FT                                {ECO:0000305}.
FT   CONFLICT    799    799       S -> N (in Ref. 2; AAP43628).
FT                                {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
//
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