CAPP1_SACHY
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 03-AUG-2022, entry version 98.
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;
OC unclassified 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 = 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 -!- 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; M86661; AAC33164.1; -; Genomic_DNA.
DR AlphaFoldDB; P29193; -.
DR SMR; P29193; -.
DR PRIDE; P29193; -.
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 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