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Database: UniProt/TrEMBL
Entry: D7KQT7_ARALL
LinkDB: D7KQT7_ARALL
Original site: D7KQT7_ARALL 
ID   D7KQT7_ARALL            Unreviewed;      1061 AA.
AC   D7KQT7;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00012305};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305};
GN   ORFNames=ARALYDRAFT_313369 {ECO:0000313|EMBL:EFH69675.1};
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   -!- 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; GL348713; EFH69675.1; -; Genomic_DNA.
DR   RefSeq; XP_002893416.1; XM_002893370.1.
DR   AlphaFoldDB; D7KQT7; -.
DR   STRING; 81972.D7KQT7; -.
DR   EnsemblPlants; fgenesh1_pm.C_scaffold_1002149; fgenesh1_pm.C_scaffold_1002149; fgenesh1_pm.C_scaffold_1002149.
DR   Gramene; fgenesh1_pm.C_scaffold_1002149; fgenesh1_pm.C_scaffold_1002149; fgenesh1_pm.C_scaffold_1002149.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   HOGENOM; CLU_006557_2_0_1; -.
DR   Proteomes; UP000008694; Unassembled WGS sequence.
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:SF42; 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          334..359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        342..357
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        728
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   1061 AA;  119148 MW;  56D8E28A92E64064 CRC64;
     MTDTTDDIAE EISFQSFEDD CKLLGSLFND VLQREVGTDF MEKIERTRVL AQSALNLRLA
     GIEDTAELLE KQLTSEISKM SLEEALTLAR AFSHFLNLMG IAETHHRVRK VCNVPQLSRS
     CNDVFSKLLQ GGISPDELYD TVCKQEVEIV LTAHPTQINR RTLQYKHIRM AHLLEYNDRP
     DLGLEDRETV IEDLVREITS LWQTDELRRQ KPTPVDEARS GLNIVEQSLW KAVPHYLRRV
     SSSLKKLTGK PLPLTCTPIK FGSWMGGDRD GNPNVKAKVT KEVSLMSRWM AIDLYIREID
     SLRFELSMNR CSDRLSRLAD EILEKEASGQ DHLECWGPNA GRSQQKFPSQ QGLSLPTQLP
     PRADLPSCTE CGESQYPKLE VPVTDYTPLN RQVKHSSKDS DICLICFVTY GQSLQIRIAN
     GTSVNSNGSQ QSLTPRGSSS SSSQLLQKKL FAESQNGRTS FQKLLEPTPP KRAGIAPYRI
     VLGEVKEKLL KTRRLLELLL EGLPCEYDPW DYYETSDQLL EPLLLCYESL QSSDAGVLAD
     GRLSDLIRRV ATFGMVLMKL DLRQEAARHS EALDAITTYL DMGTYSEWNE EKKLEFLTRE
     LKGKRPLVPP NIEVGPEVKE VLDTFRVAAE LGSESLGAYV ISMASNASDV LAVELLQKDA
     RLAVSGDLGR PCPAGTLRVV PLFETVKDLR DAGSVIRKLL SIDWYREHIQ KNHTGHQEVM
     VGYSDSGKDA GRFAAAWELY KAQEDVVAAC NEFGIKITLF HGRGGSIGRG GGPTYLAIQS
     QPPGSVMGTL RSTEQGEMVQ AKFGLPQTAV RQLEIYTTAV LLATLQPPQP PREEKWRSLM
     EDISNISCQN YRSTVYENPE FLSYFQEATP QAELGFLNIG SRPTRRKSSS GIGHLRAIPW
     VFAWTQTRFV LPAWLGVGAG LKGVCEKGHA DDLQAMYKEW PFFQSTIDLI EMVLAKADIP
     IAKHYDEELV SENRRGIGSE LRKELLTTEK YVLVISGHEK LSENNRSLKK LIESRLPYLN
     PMNMLQVEIL KRLRRDDDNN KLRDALLITI NGIAAGMRNT G
//
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