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 03-AUG-2022, entry version 127.
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}.
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; 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.AT3G14940.1; -.
DR iPTMnet; Q84VW9; -.
DR PaxDb; Q84VW9; -.
DR PRIDE; Q84VW9; -.
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; locus:2086315; AT3G14940.
DR eggNOG; ENOG502QPVS; Eukaryota.
DR HOGENOM; CLU_006557_2_0_1; -.
DR InParanoid; Q84VW9; -.
DR OMA; GPTHRFI; -.
DR OrthoDB; 775417at2759; -.
DR PhylomeDB; Q84VW9; -.
DR BioCyc; ARA:AT3G14940-MON; -.
DR BioCyc; MetaCyc:AT3G14940-MON; -.
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:0048366; P:leaf development; IBA:GO_Central.
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 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
