ID CAPP_TOBAC Reviewed; 964 AA.
AC P27154;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 08-NOV-2023, entry version 106.
DE RecName: Full=Phosphoenolpyruvate carboxylase;
DE Short=PEPC;
DE Short=PEPCase;
DE EC=4.1.1.31;
GN Name=PPC;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Samsun NN;
RX PubMed=1884006; DOI=10.1007/bf00040652;
RA Koizumi N., Sato F., Terano Y., Yamada Y.;
RT "Sequence analysis of cDNA encoding phosphoenolpyruvate carboxylase from
RT cultured tobacco cells.";
RL Plant Mol. Biol. 17:535-539(1991).
RN [2]
RP MISCELLANEOUS.
RX PubMed=11807559; DOI=10.1038/415451a;
RA Hibberd J.M., Quick W.P.;
RT "Characteristics of C4 photosynthesis in stems and petioles of C3 flowering
RT plants.";
RL Nature 415:451-454(2002).
CC -!- FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) it
CC forms oxaloacetate, a four-carbon dicarboxylic acid source for the
CC tricarboxylic acid cycle. {ECO:0000250|UniProtKB:Q9MAH0}.
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;
CC Evidence={ECO:0000250|UniProtKB:Q9MAH0};
CC -!- ACTIVITY REGULATION: By light-reversible phosphorylation.
CC {ECO:0000250}.
CC -!- PATHWAY: Photosynthesis; C4 acid pathway.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9MAH0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Tobacco, a typical C3 plant, shows characteristics of C4
CC photosynthesis in cells of stems and petioles that surround the xylem
CC and phloem. {ECO:0000269|PubMed:11807559}.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR EMBL; X59016; CAA41758.1; -; mRNA.
DR PIR; S17440; QYNT.
DR RefSeq; NP_001312166.1; NM_001325237.1.
DR AlphaFoldDB; P27154; -.
DR SMR; P27154; -.
DR STRING; 4097.P27154; -.
DR PaxDb; 4097-P27154; -.
DR ProMEX; P27154; -.
DR GeneID; 107777405; -.
DR KEGG; nta:107777405; -.
DR OrthoDB; 355614at2759; -.
DR BRENDA; 4.1.1.31; 3645.
DR UniPathway; UPA00322; -.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IBA:GO_Central.
DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW.
DR GO; GO:0048366; P:leaf development; IBA:GO_Central.
DR GO; GO:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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 PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR PANTHER; PTHR30523:SF35; PHOSPHOENOLPYRUVATE CARBOXYLASE; 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 2: Evidence at transcript level;
KW Allosteric enzyme; Carbon dioxide fixation; Cytoplasm; Lyase; Magnesium;
KW Phosphoprotein; Photosynthesis; Reference proteome.
FT CHAIN 1..964
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000166682"
FT ACT_SITE 172
FT /evidence="ECO:0000250|UniProtKB:P00864"
FT ACT_SITE 600
FT /evidence="ECO:0000250|UniProtKB:P00864"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9MAH0"
SQ SEQUENCE 964 AA; 110164 MW; 5590F35694B22DE4 CRC64;
MATRSLEKLA SIDAQLRALV PGKVSEDDKL VEYDALLLDR FLDILQDLHG EDLKETVQEC
YELSAEYEGK HDPKKLEELG NVLTSLDPGD SIVIAKAFSH MLNLANLAEE VQIAYRRRQK
LKRGDFADEN NATTESDIEE TFKKLVGDLK KSPQEVFDAL KNQTVDLVLT AHPTQSVRRS
LLQKHGRIRD CLAQLYAKDI TPDDKQELDE ALQREIQAAF RTDEIRRTAP TPQDEMRAGM
SYFHETIWKG VPKFLRRVDT ALKNIGINER LPYNAPLIQF SSWMGGDRDG NPRVTLEVTR
DVCLLARMMA ANLYYSQIEE LMFELSMWRC NDDLRIRAAE LYRSSRRDTK HYIEFWKTIP
PSEPYRVILG DVRDKLYQTR ERTRQMLAHG ISDIPEDATY NNVEQFLEPL ELCYRSLCEC
GDRPIADGSL LDFLRQVSTF GLSFVRLDIR QESDRHTDVL DAITQHLEIG SYREWSEERR
QEWLLSELSG KRPLFGPDLP RTEEIADVLD TLHVIAELPS DCFGAYIISM ATAPSDVLAV
ELLQRECHVK QPLRVVPLFE KLDDLESASA AVARLFSIEW YRNRINGKQE VMVGYSDSGK
DAGRFSAAWQ LYKAQEELIK VAKEHGVKLT MFHGRGGTVG RGGGPTHLAI LSQPPDTIQG
SLRVTVQGEV IEQSFGEEHL CFRTLQRFTA ATLEHGMHPP VSPKPEWRAL MDEIAVIATE
KYRSIVFKEP RFVEYSALAT PELEYGRMNI GSRPSKRKPS GGIESLRAIP WIFAWTQTRF
HLPVWLGFGA AFKYAIDKDI KNLRMFHEMY NEWPFFRVTI DLVEMVFAKG NPGIAALYDK
LLVSEDLLPF GELLRSNYEE TRSLLLQIAG HKDLLEGDPY LKQRLRLRDS YITTLNLLQA
YTLKRIRDPN YHVTLRPHIS KDYMESKSAA ELVQLNPTSE YAPGLEDTLI LTMKGIAAGL
QNTG
//
