ID   D7KWF8_ARALL            Unreviewed;      1032 AA.
AC   D7KWF8;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN   ORFNames=ARALYDRAFT_315894 {ECO:0000313|EMBL:EFH64938.1};
OS   Arabidopsis lyrata subsp. lyrata (Lyre-leaved rock-cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=81972 {ECO:0000313|Proteomes:UP000008694};
RN   [1] {ECO:0000313|Proteomes:UP000008694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. MN47 {ECO:0000313|Proteomes:UP000008694};
RX   PubMed=21478890; DOI=10.1038/ng.807;
RA   Hu T.T., Pattyn P., Bakker E.G., Cao J., Cheng J.-F., Clark R.M.,
RA   Fahlgren N., Fawcett J.A., Grimwood J., Gundlach H., Haberer G.,
RA   Hollister J.D., Ossowski S., Ottilar R.P., Salamov A.A., Schneeberger K.,
RA   Spannagl M., Wang X., Yang L., Nasrallah M.E., Bergelson J.,
RA   Carrington J.C., Gaut B.S., Schmutz J., Mayer K.F.X., Van de Peer Y.,
RA   Grigoriev I.V., Nordborg M., Weigel D., Guo Y.-L.;
RT   "The Arabidopsis lyrata genome sequence and the basis of rapid genome size
RT   change.";
RL   Nat. Genet. 43:476-481(2011).
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         Evidence={ECO:0000256|ARBA:ARBA00001071};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346}.
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DR   EMBL; GL348714; EFH64938.1; -; Genomic_DNA.
DR   RefSeq; XP_002888679.1; XM_002888633.1.
DR   AlphaFoldDB; D7KWF8; -.
DR   STRING; 81972.D7KWF8; -.
DR   EnsemblPlants; fgenesh1_pm.C_scaffold_2000927; fgenesh1_pm.C_scaffold_2000927; fgenesh1_pm.C_scaffold_2000927.
DR   Gramene; fgenesh1_pm.C_scaffold_2000927; fgenesh1_pm.C_scaffold_2000927; fgenesh1_pm.C_scaffold_2000927.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   HOGENOM; CLU_006557_2_0_1; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 2.
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:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 2.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008694}.
FT   REGION          373..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..408
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        154
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        699
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1032 AA;  116548 MW;  BEDDFC7E44F75D6E CRC64;
     MTDTTDDIAE EISFQSFEDD CKLLGSLFHD VLQREVGNPF MEKVERIRIL AQSALNLRMA
     GIEDTANLLE KQLTSEISKM PLEEALTLAR TFTHSLNLMG IADTHHRMHK VHNVTQLARS
     CDDIFSQLLQ SGISPEELYN TVCKQEVEIV LTAHPTQINR RTLQYKHLRI AHLLEYNTRS
     DLSLEDRETL IEDLVREITS LWQTDELRRQ KPTPVDEARA GLNIVEQSLW KAVPHYLRRV
     STSLKKFTGK PLPLTCTPIK FGSWMGGDRD GNPNVTAKVT KEVSLLSRWM AIDLYIREVD
     SLRFELSTDR CSDRFSRLAD EILEKDYDRG QSNFQKQQSS SSLPTQLPAR AHLPSCIDFG
     ESRHTKFEIA TTDYMPPNLQ KQNEQDFPES NWEKTDNGSQ SGLTSRGSFS STSQLLLQRK
     LFEESQVGKT SFQKLLEPPP LKRAGSAPYR IVLGEVKEKL VKTRRLLELL IEGLPCEYDP
     LNSYEKSDQL LEPLLLCYES LQSSGASVLA DGRLADLIRR VSTFGMVLVK LDLRQESARH
     SEALDAITTY LDMGTYSEWD EEKKLEFLTR ELKGKRPLVP PCIKVGPDVK EVLDTFRVAA
     ELGSESLGAY VISMASNASD VLAVELLQKD ARLAITSEHG KPCPGGTLRV VPLFETVNDL
     RAAGPSIRKL LSIDWYREHV QKNHNGHQEV MVGYSDSGKD AGRFTAAWEL YKAQENVVAA
     CNEFGIKITL FHGRGGSIGR GGGPTYLAIQ SQPPGSVMGS LRSTEQGEMV QAKFGIPQTA
     VRQLEVYTTA VLLATLKPPQ PPREEKWRNL MEEISTISCQ HYRSTVYENP EFLSYFHEST
     PQAELGFLNI GSRPTRRKSS SGIGHLRAIP WVFAWTQTRF VLPAWLGVGA GLKGVSEKGH
     ADDLQEMYKE WPFFQSTLEL IEMVLAKADI PMTKHYDEQL VSEKRRGLGN ELRKELMTTE
     KYVLVISGHE KLLQNNKSLK KLIESRLPYL NAMNMLQVEI LKRLRRDEDN NKLRDALLIT
     INGIAAGMRN TG
//