ID   CAPP2_SORBI             Reviewed;         960 AA.
AC   P29194;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   25-MAY-2022, entry version 104.
DE   RecName: Full=Phosphoenolpyruvate carboxylase 2;
DE            Short=PEPC 2;
DE            Short=PEPCase 2;
DE            EC=4.1.1.31;
DE   AltName: Full=CP28;
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 [GENOMIC DNA].
RX   PubMed=1840686; DOI=10.1007/bf00037146;
RA   Lepiniec L., Santi S., Keryer E., Amiet V., Vidal J., Gadal P., Cretin C.;
RT   "Complete nucleotide sequence of one member of the Sorghum
RT   phosphoenolpyruvate carboxylase gene family.";
RL   Plant Mol. Biol. 17:1077-1079(1991).
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; X59925; CAA42549.1; -; Genomic_DNA.
DR   PIR; S18240; S18240.
DR   AlphaFoldDB; P29194; -.
DR   SMR; P29194; -.
DR   STRING; 4558.Sb02g021090.1; -.
DR   eggNOG; ENOG502QPVS; Eukaryota.
DR   UniPathway; UPA00321; -.
DR   ExpressionAtlas; P29194; 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   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_0000166677"
FT   ACT_SITE        167
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        595
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   960 AA;  109547 MW;  65FDCE9B71156B18 CRC64;
     MERLSSIDAQ LRMLVPGKVS EDDKLIEYDA LLLDRFLDIL QDLHGDDLKE MVQECYEVAA
     EYETKHDLQK LDELGKMITS LDPGDSIVIA KSFSHMLNLA NLAEEVQIAY RRRIKLKKGD
     FADENSAITE SDIEETLKRL VVDLKKSPAE VFDALKSQTV DLVLTAHPTQ SVRRSLLQKH
     SRIRNCLVQL YSKDITPDDK QELDEALQRE IQAAFRTDEI RRTQPTPQDE MRAGMSYFHE
     TIWKGVPKFL RRVDTALKNI GINERVPYNA PLIQFSSWMG GDRDGNPRVT PEVTRDVCLL
     ARMMASNLYC SQIEDLMFEL SMWRCSDELR MRADELHRST KKDAKHYIEF WKKVPPNEPY
     RVILSDVRDK LYNTRERSRE LLSSGHSDIP EEATLTTVEQ LLEPLELCYR SLCACGDRVI
     ADGSLLDFLR QVSTFGLSLV RLDIRQESDR HTDVLDAITT YLGIGSYREW PEERRQEWLL
     SELNGKRPLF GPDLPKTEEI ADVLDTFHVI AELPADNFGA YIISMATAPS DVLAVELLQR
     ECHVKTPLRV VPLFEKLADL EAAPAALARL FSIDWYRQRI NGKQEVMIGY SDSGKDAGRL
     SAAWQLYKAQ EELIKVAKDF GVKLTMFHGR GGTVGRGGGP THLAILSQPP DTIHGSLRVT
     VQGEVIEQSF GEEHLSFRTL QRFTAATLEH GMHPPNAPKP EWRTLLDEMA VVATEEYRSI
     VFQEPRFVEY FRLATPETEY GRMNIGSRPS KRKPSGGIES LRAIPWIFAW TQTRFHLPVW
     LGFGGAFKHV LQKDIRNLHM LQEMYNEWPF FRVTIDLVEM VFAKGNPGIA ALYDKLLVSE
     ELRPLGEKLR ANYEETQKLL LQVAGHRDLL EGDPYLKQRL RLRDAYITTL NVCQAYTLKR
     IRDPDYHVAL RPHLSKEIMD PTKAASELVK LNPGSEYAPG LEDTLILTMK GIAAGLQNTG