ID   CAPP1_SORBI             Reviewed;         960 AA.
AC   P29195;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Phosphoenolpyruvate carboxylase 1;
DE            Short=PEPC 1;
DE            Short=PEPCase 1;
DE            EC=4.1.1.31;
DE   AltName: Full=CP21;
GN   Name=PEPC;
OS   Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX   NCBI_TaxID=4558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Root;
RX   PubMed=2022326; DOI=10.1016/0378-1119(91)90037-c;
RA   Cretin C., Santi S., Keryer E., Lepiniec L., Tagu D., Vidal J., Gadal P.;
RT   "The phosphoenolpyruvate carboxylase gene family of Sorghum: promoter
RT   structures, amino acid sequences and expression of genes.";
RL   Gene 99:87-94(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8443342; DOI=10.1007/bf00028806;
RA   Lepiniec L., Keryer E., Philippe H., Gadal P., Cretin C.;
RT   "Sorghum phosphoenolpyruvate carboxylase gene family: structure, function
RT   and molecular evolution.";
RL   Plant Mol. Biol. 21:487-502(1993).
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; 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; X55664; CAA39197.1; -; mRNA.
DR   EMBL; X65137; CAA46267.1; -; Genomic_DNA.
DR   PIR; JH0381; JH0381.
DR   PIR; S31159; S31159.
DR   AlphaFoldDB; P29195; -.
DR   SMR; P29195; -.
DR   STRING; 4558.Sb04g008720.1; -.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   SABIO-RK; P29195; -.
DR   UniPathway; UPA00321; -.
DR   ExpressionAtlas; P29195; baseline and differential.
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   2: Evidence at transcript level;
KW   Allosteric enzyme; Carbon dioxide fixation; Cytoplasm; Lyase; Magnesium;
KW   Phosphoprotein; Photosynthesis.
FT   CHAIN           1..960
FT                   /note="Phosphoenolpyruvate carboxylase 1"
FT                   /id="PRO_0000166676"
FT   ACT_SITE        168
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        596
FT                   /evidence="ECO:0000250"
FT   MOD_RES         7
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   960 AA;  109439 MW;  73927283CE3298AA CRC64;
     MPERHQSIDA QLRLLAPGKV SEDDKLVEYD ALLVDRFLDI LQDLHGPHLR EFVQECYELS
     AEYENDRDEA RLGELGSKLT SLPPGDSIVV ASSFSHMLNL ANLAEEVQVA QRRRIKLKRG
     DFADEASAPT ESDIEETLKR LVSQLGKSRE EVFDALKNQT VDLVFTAHPT QSVRRSLLQK
     HGRIRNCLRQ LYAKDITADD KQELDEALQR EIQAAFRTDE IRRTPPTPQD EMRAGMSYFH
     ETIWKGVPKF LRRIDTALKN IGINERLPYN APLIQFSSWM GGDRDGNPRV TPEVTRDVCL
     LARMMAANLY FSQIEDLMFE LSMWRCSDEL RIRADELHRS SKRAAKHYIE FWKQVPPNEP
     YRVILGDVRD KLYYTRERSR HLLSSGISEI PEEATFTNVE QFLEPLELCY RSLCACGDKP
     IADGSLLDFL RQVFNFGLAL VKLDIRQESD RHTDVLDSIT THLGIGSYAE WSEEKRQDWL
     LSELRGKRPL FGSDLPQTEE TADVLGTFHV LAELPADCFG AYIISMATAP SDVLAVELLQ
     RECHVKQPLR VVPLFEKLAD LEAAPAAVAR LFSIDWYMNR INGKQEVMIG YSDSGKDAGR
     LSAAWQMYKA QEELIKVAKH YGVKLTMFHG RGGTVGRGGG PTHLAILSQP PDTIHGSLRV
     TVQGEVIEHS FGEELLCFRT LQRYTAATLE HGMHPPISPK PEWRALMDEM AVVATKEYRS
     IVFQEPRFVE YFRSATPETE YGRMNIGSRP SKRKPSGGIE SLRAIPWIFA WTQTRFHLPV
     WLGFGAAIKH IMQKDIRNIH VLKEMYNEWP FFRVTLDLLE MVFAKGDPGI AAVYDKLLVA
     EDLQSFGEQL RKNYEETKEL LLQVAGHKDV LEGDPYLKQR LRLRESYITT LNVCQAYTLK
     RIRDPSFQVS PQPPLSKEFT DESQPVELVQ LNQQSEYAPG LEDTLILTMK GIAAGMQNTG