ID   CAPP1_SACHY             Reviewed;         966 AA.
AC   P29193;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   02-SEP-2026, entry version 108.
DE   RecName: Full=Phosphoenolpyruvate carboxylase, housekeeping isozyme;
DE            Short=PEPC;
DE            Short=PEPCase;
DE            EC=4.1.1.31;
OS   Saccharum hybrid (Sugarcane).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Saccharinae; Saccharum.
OX   NCBI_TaxID=15819;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1450381; DOI=10.1007/bf00046451;
RA   Albert H.A., Martin T., Sun S.S.;
RT   "Structure and expression of a sugarcane gene encoding a housekeeping
RT   phosphoenolpyruvate carboxylase.";
RL   Plant Mol. Biol. 20:663-671(1992).
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 = phosphoenolpyruvate +
CC         hydrogencarbonate; 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   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M86661; AAC33164.1; -; Genomic_DNA.
DR   AlphaFoldDB; P29193; -.
DR   SMR; P29193; -.
DR   GO; GO:0048046; C:apoplast; IEA:TreeGrafter.
DR   GO; GO:0009507; C:chloroplast; IEA:TreeGrafter.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015977; P:carbon fixation; IEA:InterPro.
DR   GO; GO:0048366; P:leaf development; IEA:TreeGrafter.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   FunFam; 1.20.1440.90:FF:000001; Phosphoenolpyruvate carboxylase 1; 1.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
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   NCBIfam; NF000584; PRK00009.1; 1.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF33; PHOSPHOENOLPYRUVATE CARBOXYLASE 3; 1.
DR   Pfam; PF00311; PEPcase; 1.
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   Allosteric enzyme; Carbon dioxide fixation; Cytoplasm; Lyase; Magnesium;
KW   Phosphoprotein; Photosynthesis.
FT   CHAIN           1..966
FT                   /note="Phosphoenolpyruvate carboxylase, housekeeping
FT                   isozyme"
FT                   /id="PRO_0000166675"
FT   ACT_SITE        172
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        601
FT                   /evidence="ECO:0000250"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   966 AA;  110219 MW;  FD84762318FED073 CRC64;
     MARNAVDKAT SIDAQLRLLA PQKLSDDDKL VEYDALLLDR FLDILQDLHG EDIRETVQEC
     YELAAEYENK LDPKMLDEIG NVLTSLDPGD SIVITKSFSH MLILANLAEE VQIAYRRRIK
     LKKGDFVDEN SATTESDIEE TLKRLMHQLK KSPLEVFDAL KNQTVDLVLT AHPTQSVRRS
     LLQKHGRIRN CLTQLYAKDI TPDEKQELDE ALQREIQAAF RTDEIRRAPP TPQDEMRAGM
     SYFHETIWKG VPKFLRRVDT ALKNIGINER LPYNAPIIQF SSWMGGDRDG NPRVTPEITR
     DVCLLARMMA ANLYNAQIED LMFELSMWRC SDELRVKVDE LHRSSKKDTT KHYIEFWKQV
     PPSEPYRVIL SDVRDKLYNT RERARHLLAS GFSEIPEEAT FTDVEQFLEP LELCYRSLCA
     CGDRSVADGS LLDFLRQVST FGLSLVRLDI RQESDRHTDV MDAITEYLGI GSYRKWTEEK
     RQEWLLSELN GKRPLFGPDL PKSDEIADVL DTFHVLAELP SDSFGAYVIS MATAPSDVLA
     VELLQRECHV KKPLRVVPLF EKLADLEAAP AALARLFSVE WYRNRINGKQ EVMIGYSDSG
     KDAGRFSAAW QLYKAQEELI NVAKLYGVKL TMFHGRGGTV GRGGGPTHLA ILSQPPETIH
     GSLRVTVQGE VIEQSFGEEH LCFRTLQRFT AATLEHGMHP PISPKPEWRA LMDEMAIVAT
     KEYRSIVFEE PRFVEYFRLA TPEMEYGRMN IGSRPSKRKP SAGIESLRAI PWIFAWTQTR
     FHLPVWLGFG AAFKHVLDKD IRNLQTLQEM YNQWPFFRVT IDLVEMVFAK GDPGIAALYD
     KLLVSEDLWS FGKRLRANYE ETKQLLLQVA GHKDLLEGDP YLKQRLRIRD SYITALNVCQ
     AYMLKRIRDP GFQVNPGPHL SKDIMDMGKP ASELVKLNTT SEYAPGLEDT LILTMKGIAA
     GMQNTG
//