CAPP3_SORBI
ID CAPP3_SORBI Reviewed; 960 AA.
AC P15804;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 25-MAY-2022, entry version 124.
DE RecName: Full=Phosphoenolpyruvate carboxylase 3;
DE Short=PEPC 3;
DE Short=PEPCase 3;
DE EC=4.1.1.31;
DE AltName: Full=CP46;
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 STRAIN=cv. Tamaran FNK 140; TISSUE=Leaf;
RX PubMed=2308851; DOI=10.1093/nar/18.3.658;
RA Cretin C., Keryer E., Tagu D., Lepiniec L., Vidal J., Gadal P.;
RT "Complete cDNA sequence of sorghum phosphoenolpyruvate carboxylase involved
RT in C4 photosynthesis.";
RL Nucleic Acids Res. 18:658-658(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE, AND SEQUENCE REVISION.
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 [3]
RP NUCLEOTIDE SEQUENCE, AND SEQUENCE REVISION.
RC TISSUE=Root;
RX PubMed=1623186; DOI=10.1007/bf00027358;
RA Lepiniec L., Keryer E., Tagu D., Gadal P., Cretin C.;
RT "Complete nucleotide sequence of a sorghum gene coding for the
RT phosphoenolpyruvate carboxylase involved in C4 photosynthesis.";
RL Plant Mol. Biol. 19:339-342(1992).
RN [4]
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).
RN [5]
RP PHOSPHORYLATION AT SER-8.
RX PubMed=16668168; DOI=10.1104/pp.96.1.297;
RA Jiao J.-A., Vidal J., Echevarria C., Chollet R.;
RT "In vivo regulatory phosphorylation site in C4-leaf phosphoenolpyruvate
RT carboxylase from maize and sorghum.";
RL Plant Physiol. 96:297-301(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 -!- ACTIVITY REGULATION: By light-reversible phosphorylation.
CC -!- PATHWAY: Photosynthesis; C4 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; X17379; CAA35251.2; -; mRNA.
DR EMBL; X63756; CAA45284.1; -; Genomic_DNA.
DR PIR; S08216; QYMG.
DR PIR; S22507; S22507.
DR AlphaFoldDB; P15804; -.
DR SMR; P15804; -.
DR STRING; 4558.Sb10g021330.1; -.
DR iPTMnet; P15804; -.
DR eggNOG; ENOG502QPVS; Eukaryota.
DR BRENDA; 4.1.1.31; 5768.
DR SABIO-RK; P15804; -.
DR UniPathway; UPA00322; -.
DR ExpressionAtlas; P15804; 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 1: Evidence at protein level;
KW Allosteric enzyme; Carbon dioxide fixation; Cytoplasm; Lyase; Magnesium;
KW Phosphoprotein; Photosynthesis.
FT CHAIN 1..960
FT /note="Phosphoenolpyruvate carboxylase 3"
FT /id="PRO_0000166678"
FT ACT_SITE 167
FT /evidence="ECO:0000250"
FT ACT_SITE 597
FT /evidence="ECO:0000250"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16668168"
SQ SEQUENCE 960 AA; 108372 MW; AE84FE6FDA214403 CRC64;
MASERHHSID AQLRALAPGK VSEELIQYDA LLVDRFLDIL QDLHGPSLRE FVQECYEVSA
DYEGKKDTSK LGELGAKLTG LAPADAILVA SSILHMLNLA NLAEEVELAH RRRNSKLKHG
DFSDEGSATT ESDIEETLKR LVSLGKTPAE VFEALKNQSV DLVFTAHPTQ SARRSLLQKN
ARIRNCLTQL SAKDVTVEDK KELDEALHRE IQAAFRTDEI RRAQPTPQDE MRYGMSYIHE
TVWNGVPKFL RRVDTALKNI GINERLPYDV PLIKFCSWMG GDRDGNPRVT PEVTRDVCLL
SRMMAANLYI NQVEDLMFEL SMWRCNDELR ARAEEVQSTP ASKKVTKYYI EFWKQIPPNE
PYRVILGAVR DKLYNTRERA RHLLATGFSE ISEDAVFTKI EEFLEPLELC YKSLCECGDK
AIADGSLLDL LRQVFTFGLS LVKLDIRQES ERQTDVIDAI TTHLGIGSYR SWPEDKRMEW
LVSELKGKRP LLPPDLPMTE EIADVIGAMR VLAELPIDSF GPYIISMCTA PSDVLAVELL
QRECGIRQTL PVVPLFERLA DLQAAPASVE KLFSTDWYIN HINGKQQVMV GYSDSGKDAG
RLSAAWQLYV AQEEMAKVAK KYGVKLTLFH GRGGTVGRGG GPTHLAILSQ PPDTINGSIR
VTVQGEVIEF MFGEENLCFQ SLQRFTAATL EHGMHPPVSP KPEWRKLMEE MAVVATEEYR
SVVVKEPRFV EYFRSATPET EYGKMNIGSR PAKRRPGGGI TTLRAIPWIF SWTQTRFHLP
VWLGVGAAFK WAIDKDIKNF QKLKEMYNEW PFFRVTLDLL EMVFAKGDPG IAGLYDELLV
AEELKPFGKQ LRDKYVETQQ LLLQIAGHKD ILEGDPYLKQ GLRLRNPYIT TLNVFQAYTL
KRIRDPSFKV TPQPPLSKEF ADENKPAGLV KLNGERVPPG LEDTLILTMK GIAAGMQNTG
