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