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Database: UniProt/SWISS-PROT
Entry: CAPP3_ARATH
LinkDB: CAPP3_ARATH
Original site: CAPP3_ARATH 
ID   CAPP3_ARATH             Reviewed;         968 AA.
AC   Q84VW9; O81357; Q0WTJ7;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   24-JAN-2024, entry version 133.
DE   RecName: Full=Phosphoenolpyruvate carboxylase 3;
DE            Short=AtPPC3;
DE            Short=PEPC 3;
DE            Short=PEPCase 3;
DE            EC=4.1.1.31;
GN   Name=PPC3; Synonyms=PEPC, PPC; OrderedLocusNames=At3g14940;
GN   ORFNames=K15M2.8;
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].
RC   STRAIN=cv. Columbia;
RA   Paterson K.M., Nimmo H.G.;
RT   "Arabidopsis thaliana phosphoenolpyruvate carboxylase full-length cDNA.";
RL   Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Columbia; TISSUE=Seedling;
RA   Hartung F.;
RT   "Genomic structure of PEPC in Arabidopsis thaliana.";
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA   Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT   features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT   clones.";
RL   DNA Res. 7:217-221(2000).
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   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   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   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).
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 roots and siliques, and to a lower
CC       extent in stems, leaves and flowers. {ECO:0000269|PubMed:12805623}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR   EMBL; AF071788; AAC24594.1; -; mRNA.
DR   EMBL; AJ131710; CAA10486.1; -; Genomic_DNA.
DR   EMBL; AP000370; BAA97057.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE75592.1; -; Genomic_DNA.
DR   EMBL; CP002686; ANM64773.1; -; Genomic_DNA.
DR   EMBL; BT004642; AAO42888.1; -; mRNA.
DR   EMBL; AK227556; BAE99551.1; -; mRNA.
DR   PIR; T52186; T52186.
DR   RefSeq; NP_001326778.1; NM_001338141.1.
DR   RefSeq; NP_188112.1; NM_112356.4.
DR   PDB; 5FDN; X-ray; 2.20 A; A/B=1-968.
DR   PDBsum; 5FDN; -.
DR   AlphaFoldDB; Q84VW9; -.
DR   SMR; Q84VW9; -.
DR   BioGRID; 6057; 9.
DR   STRING; 3702.Q84VW9; -.
DR   iPTMnet; Q84VW9; -.
DR   PaxDb; 3702-AT3G14940-1; -.
DR   ProteomicsDB; 239094; -.
DR   EnsemblPlants; AT3G14940.1; AT3G14940.1; AT3G14940.
DR   EnsemblPlants; AT3G14940.2; AT3G14940.2; AT3G14940.
DR   GeneID; 820723; -.
DR   Gramene; AT3G14940.1; AT3G14940.1; AT3G14940.
DR   Gramene; AT3G14940.2; AT3G14940.2; AT3G14940.
DR   KEGG; ath:AT3G14940; -.
DR   Araport; AT3G14940; -.
DR   TAIR; AT3G14940; PPC3.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   HOGENOM; CLU_006557_2_0_1; -.
DR   InParanoid; Q84VW9; -.
DR   OMA; WAQYETQ; -.
DR   OrthoDB; 355614at2759; -.
DR   PhylomeDB; Q84VW9; -.
DR   BioCyc; ARA:AT3G14940-MONOMER; -.
DR   BioCyc; MetaCyc:AT3G14940-MONOMER; -.
DR   BRENDA; 4.1.1.31; 399.
DR   PRO; PR:Q84VW9; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q84VW9; baseline and differential.
DR   Genevisible; Q84VW9; AT.
DR   GO; GO:0005829; C:cytosol; 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:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
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; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF33; PHOSPHOENOLPYRUVATE CARBOXYLASE 3; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Allosteric enzyme; Carbon dioxide fixation; Cytoplasm; Lyase;
KW   Magnesium; Phosphoprotein; Photosynthesis; Reference proteome.
FT   CHAIN           1..968
FT                   /note="Phosphoenolpyruvate carboxylase 3"
FT                   /id="PRO_0000166659"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        603
FT                   /evidence="ECO:0000250"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9MAH0"
FT   MOD_RES         705
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9MAH0"
FT   CONFLICT        245
FT                   /note="H -> R (in Ref. 5; AAO42888 and 6; BAE99551)"
FT                   /evidence="ECO:0000305"
FT   HELIX           30..49
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           51..70
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           73..84
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           88..115
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           127..131
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   TURN            133..135
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           139..150
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           154..162
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   STRAND          165..170
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           180..196
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           203..221
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           233..240
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           243..246
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           248..264
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   TURN            265..267
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   STRAND          278..283
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   TURN            285..287
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           297..325
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           333..340
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           366..391
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           398..400
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           405..421
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           425..428
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           431..442
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   TURN            443..445
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   STRAND          446..454
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           455..468
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           475..477
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           480..492
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           506..520
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           523..525
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   STRAND          526..532
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           537..549
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   STRAND          557..562
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           565..580
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           582..588
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   STRAND          591..596
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           598..605
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           607..628
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   STRAND          631..636
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           641..643
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           648..654
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   STRAND          664..669
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           671..678
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           681..700
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           708..729
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           735..742
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           745..750
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   TURN            766..768
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           771..780
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           785..788
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           791..801
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           805..815
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           817..831
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           835..845
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           848..850
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           851..872
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   TURN            877..880
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           882..910
FT                   /evidence="ECO:0007829|PDB:5FDN"
FT   HELIX           949..964
FT                   /evidence="ECO:0007829|PDB:5FDN"
SQ   SEQUENCE   968 AA;  110160 MW;  1CECE8B8981F63F0 CRC64;
     MAGRNIEKMA SIDAQLRQLV PAKVSEDDKL VEYDALLLDR FLDILQDLHG EDLRETVQEL
     YELSAEYEGK REPSKLEELG SVLTSLDPGD SIVISKAFSH MLNLANLAEE VQIAHRRRIK
     KLKKGDFVDE SSATTESDIE ETFKRLVSDL GKSPEEIFDA LKNQTVDLVL TAHPTQSVRR
     SLLQKHGRIR DCLAQLYAKD ITPDDKQELD ESLQREIQAA FRTDEIRRTP PTPQDEMRAG
     MSYFHETIWK GVPKFLRRVD TALKNIGIDE RVPYNAPLIQ FSSWMGGDRD GNPRVTPEVT
     RDVCLLARMM AANLYYNQIE NLMFELSMWR CTDEFRVRAD ELHRNSRKDA AKHYIEFWKT
     IPPTEPYRVI LGDVRDKLYH TRERSRQLLS NGISDIPEEA TFTNVEQFLE PLELCYRSLC
     SCGDSPIADG SLLDFLRQVS TFGLSLVRLD IRQESERHTD VLDAITKHLD IGSSYRDWSE
     EGRQEWLLAE LSGKRPLFGP DLPKTEEISD VLDTFKVISE LPSDCFGAYI ISMATSPSDV
     LAVELLQREC HVKNPLRVVP LFEKLADLEA APAAVARLFS IDWYKNRING KQEVMIGYSD
     SGKDAGRLSA AWELYKAQEE LVKVAKKYGV KLTMFHGRGG TVGRGGGPTH LAILSQPPDT
     VNGSLRVTVQ GEVIEQSFGE AHLCFRTLQR FTAATLEHGM NPPISPKPEW RALLDEMAVV
     ATEEYRSVVF QEPRFVEYFR LATPELEYGR MNIGSRPSKR KPSGGIESLR AIPWIFAWTQ
     TRFHLPVWLG FGAAFRYAIK KDVRNLHMLQ DMYKQWPFFR VTIDLIEMVF AKGDPGIAAL
     YDKLLVSEDL WAFGEKLRAN FDETKNLVLQ TAGHKDLLEG DPYLKQRLRL RDSYITTLNV
     CQAYTLKRIR DANYNVTLRP HISKEIMQSS KSAQELVKLN PTSEYAPGLE DTLILTMKGI
     AAGLQNTG
//
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