CAPP_PICAB
ID CAPP_PICAB Reviewed; 963 AA.
AC P51063;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Phosphoenolpyruvate carboxylase;
DE Short=PEPC;
DE Short=PEPCase;
DE EC=4.1.1.31;
GN Name=PPC;
OS Picea abies (Norway spruce) (Picea excelsa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3329;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cotyledon, and Stem;
RA Relle M., Sutter A., Wild A.;
RT "A method to isolate cDNA-quality RNA from adult conifer needles and a psbA
RT cDNA from Norway spruce.";
RL J. Plant Physiol. 149:225-228(1996).
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 -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR EMBL; X79090; CAA55700.1; -; mRNA.
DR PIR; S49344; S49344.
DR AlphaFoldDB; P51063; -.
DR SMR; P51063; -.
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..963
FT /note="Phosphoenolpyruvate carboxylase"
FT /id="PRO_0000166674"
FT ACT_SITE 172
FT /evidence="ECO:0000250"
FT ACT_SITE 600
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 963 AA; 109552 MW; DF9C63F77E179FD4 CRC64;
MARNNLEKMA SIDAQMRLLV PGKVSEDDKL IEYDALLLDR FLDILQDLHG EDIRAMVQEC
YERSGEYEGK NDPHKLEELG NVLTSLDPGD SIVVASSFSH MLNLANLAEE VQIAYRRRNK
IKRGGFADES NATTESDIEE TFKRLVNQLG KSPAEVFDAL KNQTVDLVLT AHPTQSVRRS
LLQKHARIRN CLSQLYGKDI TPDEKQELDE ALLREIQAAF RTDEIRRTPP TPQDEMRAGM
SYFHETIWKG VPKFLRRIDT ALKSIGINER VPYNAPLIQF SSWMGGDRDG NPRVTPEVTR
DVCLLARMMA ANLYYSQIED LMFELSMWRC SDELRARALQ LHSASKKDAK HYIEFWKQIP
PNEPFRVILG DVRDKLYNTR ERTRQLLSNG ISDIPEEVTF TNIDEFLEPL ELCYRSLCST
GDQPIADGSL LDFMRQVSTF GLSFVKLDIR QESDRHSDVA DAITRHLGIG SYKEWSEEQR
QAWLLSELQG KRPLFGPDLP KTDEVRDVLD TFHVISELPA DNFGAYIISM ATAASDVLVV
ELLQRECHVK KPLRVVPLFE KLADLEAAPA ALARLFSINW YRNRIDGKQE VMIGYSDSGK
DAGRLSAGWA LYKAQEDLIK VAKEFGIKLT MFHGRGGTVG RGGGPTHLAI LSQPPDTIHG
SFRVTVQGEV IEQSFGEEHL CFRTLQRFTA ATLEHGMRPP VAPKPEWREL MDEMAVVATK
EYRSIVFQDP RFVEYFRSAT PELEYGRMNI GSRPSKRKPS GGIESLRAIP WIFAWTQTRF
HLPVWLGFGA AFKHVMEKDI RNLHMLQQMY NEWPFFRVTI DLIEMVFAKG DPGIAALYDK
LLVSDDLWAI GEKLRANYGE TKDLLLQVAG HKDLLEGDPY LKQRLRLRDS YITTLNVCQA
YTLKRIRDPN YHVNLRPHLS KESSTKPAAE LVKLNPTSEY APGLEDTLIL TMKGIAAGMQ
NTG