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CAPP2_MESCR
ID   CAPP2_MESCR             Reviewed;         960 AA.
AC   P16097;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Phosphoenolpyruvate carboxylase 2;
DE            Short=PEPC 2;
DE            Short=PEPCase 2;
DE            EC=4.1.1.31;
GN   Name=PPC2;
OS   Mesembryanthemum crystallinum (Common ice plant) (Cryophytum crystallinum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Aizoaceae; Mesembryanthemum;
OC   Mesembryanthemum subgen. Cryophytum.
OX   NCBI_TaxID=3544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2780305; DOI=10.1093/nar/17.16.6743;
RA   Cushman J.C., Bohnert H.J.;
RT   "Nucleotide sequence of the Ppc2 gene encoding a housekeeping isoform of
RT   phosphoenolpyruvate carboxylase from Mesembryanthemum crystallinum.";
RL   Nucleic Acids Res. 17:6743-6744(1989).
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   -!- PATHWAY: Photosynthesis; C3 acid pathway.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR   EMBL; X14588; CAA32728.2; -; Genomic_DNA.
DR   PIR; S05550; QYIX2.
DR   AlphaFoldDB; P16097; -.
DR   SMR; P16097; -.
DR   UniPathway; UPA00321; -.
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: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   3: Inferred from homology;
KW   Allosteric enzyme; Carbon dioxide fixation; Cytoplasm; Lyase; Magnesium;
KW   Photosynthesis.
FT   CHAIN           1..960
FT                   /note="Phosphoenolpyruvate carboxylase 2"
FT                   /id="PRO_0000166671"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        593
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   960 AA;  109184 MW;  5318B18E37B76B5A CRC64;
     MASIDAQLRL LVPAKVSEDD KLVEYDALLL DRFLDILQDL HGEDIRETVQ ECYERSAEYE
     GKHDPKKLDE LGSVLTSLDA GDSIVVAKSF SHMLNLANLA EEVQIAYRRR IKKLKKGDLS
     DENSATTESD IEETFKRLVA ELGKSPEEIF DALKNQTVDL VFTAHPTQSV RRSLLQKHGR
     IRNCLAQLYA KDITPDDKQE LDEALQREIQ AAFRTDEIRR TPPTPQDEMR AGMSYFHETI
     WKGVPKFLRR VDTALKNIGI NERVPYNAPL IQFSSWMGGD RDGNPRVTPE VTRDVCLLAR
     MMAANLYFSQ IEDLMFELSM WRCTDELRAR ADELHSSSRR DAKHYIEFWK HIPPNEPYRV
     ILGDVRDKLY NTRERSRQML SHGVSDIPED ATYTSLEQFL EPLELCYGSL CACGDRPIAD
     GTLLDFLRQV FTFGLSLVRL DIRQESDRHT DVMDAITQHL EIGSYKEWSE EKRQEWLLSE
     LSGKRPLFGS DLPQTEEIAD VLDTLHVLAE LPSDCFGAYI ISMATSPSDV LAVELLQREC
     RVKQPLRVVP LFEKLADLEA APAAVARLFS IDWYKNRING KQEVMIGYSD SGKDAGRLSA
     AWALYKAQEE LVQVAKEYGV KLTMFHGRGG TVGRGGGPTH LAILSQPPET VNGSLRVTVQ
     GEVIEQSFGE EHLCFRTLQR FTAATLEHGM HPPISPKPEW RALLDEIAVV ATEKYRSIVF
     KEPRFVEYFR LATPELEYGR MNIGSRPSKR KPSGGIESLR AIPWIFAWTQ TRFHLPVWLG
     FGAAFGYAIQ KDVKNLSVLQ KMYNEWPFFR VTIDLVEMVF AKGDPGIAAL YDKLLVSEEL
     WPFGERLRAD FEETKGLILK IAGHKDLLEG DPYLRQRLRL RDSYITTLNA LQAYTLKRIR
     DPNYNVQLRP HISKEYMDST SNKPAAELVK LNPSSEYAPG LEDTLILTMK GIAAGMQNTG
 
 
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