ID   CAPP_AMAHP              Reviewed;         964 AA.
AC   Q43299;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Phosphoenolpyruvate carboxylase;
DE            Short=PEPC;
DE            Short=PEPCase;
DE            EC=4.1.1.31;
OS   Amaranthus hypochondriacus (Prince-of-Wales feather) (Amaranthus hybridus
OS   var. hypochondriacus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Amaranthaceae; Amaranthus.
OX   NCBI_TaxID=28502;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RA   Rydzik E., Berry J.;
RT   "The C4 phosphoenolpyruvate carboxylase (PEPCase) from grain Amaranth.";
RL   (er) Plant Gene Register PGR95-135(1995).
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   -!- PATHWAY: Photosynthesis; C4 acid pathway.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR   EMBL; Z68125; CAA92209.1; -; mRNA.
DR   EMBL; L49175; AAB18633.1; -; mRNA.
DR   AlphaFoldDB; Q43299; -.
DR   SMR; Q43299; -.
DR   PRIDE; Q43299; -.
DR   BRENDA; 4.1.1.31; 286.
DR   UniPathway; UPA00322; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IDA:CACAO.
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   2: Evidence at transcript level;
KW   Allosteric enzyme; Carbon dioxide fixation; Cytoplasm; Lyase; Magnesium;
KW   Phosphoprotein; Photosynthesis.
FT   CHAIN           1..964
FT                   /note="Phosphoenolpyruvate carboxylase"
FT                   /id="PRO_0000166656"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        600
FT                   /evidence="ECO:0000250"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   964 AA;  109480 MW;  3D49C2DE8BDE11B3 CRC64;
     MASGKVEKMA SIDAQLRLLA PKKVSEDDKL VEYDALLLDR FLDILESLHG SGIRETVQEL
     YEHAAEYERT HDTKKLEELG NLITSLDAGD SIVIAKSFSQ MLNLANLAEE VQLAYRRRIK
     KTKKGDFADE SSAITESDFE ETLRRLVDLK KSPEEIFATL KNQTVDLVLT AHPTQSVRRS
     LLQKHGRIRD CLSQLYAKDI SPDDKQELDE ALQRAIQAAF RTDEIRRVQP TPQDEMRMGM
     SYFHETIWKG VPKFLRRVDT ALKNIGINER VPYNVPLIQF SSWMGGDRDG NPRVTPEVTR
     DVVLLARMMA ANMYFTQITD LMFELSMWRC NDEVRARAQE LHSQSKSDAK HYIEFWKQIP
     LSEPYRVILG DVRDKLYNTR EHAHKLLANG SSDVPEESTF THIDQFLEPL ELCYKSLCAS
     GDQPIADGSL LDFMRQVSTF GLSLVKLDIR QESDRHTEVM DAITTHLGIG SYRSWSEEKR
     QEWLLSELRG KRPLFGSDLP MSYEVADAIG TFRVLAELPN DSFGAYIISM ATAPSDVLAV
     ELLQRECGIK KPLRVVPLFE KLADLQSAAA SMTRLFSIDW YKNRINGTQE VMIGYSDSGK
     DAGRLSAAWQ LYKVQEQLIQ VAKEYGVKLT MFHGRGGTVG RGGGPTHLAL LSQPPDTIHG
     SLRVTIQGEV IEQSFGEEHL CFRTLERYTA ATLEHGIDPP TSPKPEWRAL MDEMAVITTK
     EYRSVVLQEP RFVEYFRSAT PELEYGRMNI GSRPAKRKPG GGIETLRAIP WIFSWTQTRF
     HLPVWLGCGA AFKHVIEKDI KNLAMLKDMY NQWSFFRVTI DLLEMVFAKG DPGIAALYDK
     LLVKDELKPF GENLRKSYLE AQKFLLEIAG HKDPLDADPY LKQILRLRDP YTTTLNVFQV
     YTLKRIRDPS FHVTVRPHLS KEMDANSLAA DLVKLNPTSE YPPGLEDTLI LTMKGIAAGM
     QNTG