CAPPB_FLATR
ID CAPPB_FLATR Reviewed; 965 AA.
AC Q9FV66;
DT 11-JAN-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Phosphoenolpyruvate carboxylase 1 {ECO:0000303|PubMed:12111227};
DE Short=PEPC 1 {ECO:0000303|PubMed:12111227};
DE Short=PEPCase 1 {ECO:0000303|PubMed:12111227};
DE Short=ppcB {ECO:0000303|PubMed:9225854};
DE EC=4.1.1.31 {ECO:0000269|PubMed:12111227};
GN Name=PPCB {ECO:0000303|PubMed:9225854};
OS Flaveria trinervia (Clustered yellowtops) (Oedera trinervia).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Tageteae; Flaveria.
OX NCBI_TaxID=4227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
RC TISSUE=Root;
RX PubMed=12111227; DOI=10.1007/s00425-002-0757-x;
RA Blasing O.E., Ernst K., Streubel M., Westhoff P., Svensson P.;
RT "The non-photosynthetic phosphoenolpyruvate carboxylases of the C4 dicot
RT Flaveria trinervia -- implications for the evolution of C4
RT photosynthesis.";
RL Planta 215:448-456(2002).
RN [2]
RP TISSUE SPECIFICITY, AND INDUCTION BY GLUCOSE.
RX PubMed=9225854; DOI=10.1023/a:1005838020246;
RA Ernst K., Westhoff P.;
RT "The phosphoenolpyruvate carboxylase (ppc) gene family of Flaveria
RT trinervia (C4) and F. pringlei (C3): molecular characterization and
RT expression analysis of the ppcB and ppcC genes.";
RL Plant Mol. Biol. 34:427-443(1997).
CC -!- FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) it
CC forms oxaloacetate, a four-carbon dicarboxylic acid source for the
CC tricarboxylic acid cycle. May be involved in phloem loading with
CC sucrose and in anions and cations uptake and amino acid biosynthesis in
CC roots. {ECO:0000269|PubMed:12111227}.
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 Evidence={ECO:0000269|PubMed:12111227};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9MAH0};
CC -!- ACTIVITY REGULATION: Activated by the allosteric regulator glucose-6-
CC phosphate (By similarity). Inhibited by malate and aspartate (By
CC similarity). Up regulated by light-reversible phosphorylation (By
CC similarity). {ECO:0000250|UniProtKB:P04711,
CC ECO:0000250|UniProtKB:P30694}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=83 umol/min/mg enzyme {ECO:0000269|PubMed:12111227};
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q9MAH0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P27154}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and stems and at low levels in
CC leaves. Preferentially expressed in the phloem and in root tips.
CC {ECO:0000269|PubMed:9225854}.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR EMBL; AF248079; AAG17618.1; -; mRNA.
DR AlphaFoldDB; Q9FV66; -.
DR SMR; Q9FV66; -.
DR PRIDE; Q9FV66; -.
DR SABIO-RK; Q9FV66; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IDA:UniProtKB.
DR GO; GO:0015977; P:carbon fixation; IDA:UniProtKB.
DR GO; GO:0009915; P:phloem sucrose loading; TAS:UniProtKB.
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 Carbon dioxide fixation; Cytoplasm; Lyase; Magnesium; Phosphoprotein.
FT CHAIN 1..965
FT /note="Phosphoenolpyruvate carboxylase 1"
FT /id="PRO_0000403439"
FT ACT_SITE 172
FT /evidence="ECO:0000250|UniProtKB:P04711"
FT ACT_SITE 600
FT /evidence="ECO:0000250|UniProtKB:P04711"
FT ACT_SITE 641
FT /evidence="ECO:0000250|UniProtKB:P04711"
FT BINDING 283
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 450
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 597
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 635
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 641
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 665
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 673
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 753
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 767..769
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 829
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 888
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 963
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P04711"
SQ SEQUENCE 965 AA; 110413 MW; 56647B9905A5DA2C CRC64;
MANRNLEKLA SIDAHLRLLV PGKVSEDDKL IEYDALLLDK FLDILQDLHG EDLKETVQEC
YELSAEYEGK RDPKKLEELG SVLTSLDPGD SIVIAKAFSH MLNLANLAEE VQIAYRRRIK
LKKGDFADEA HATTESDMEE TLKKLVYKLN KSPEEVFDAL KNQTVDLVLT AHPTQSVRRS
LLQKHGRIRN CLAQLYAKDI TPDDKQELDE ALHREIQAAF RTDEIRRTQP TPQDEMRAGM
SYFHETIWKG VPKFLRRVDT ALKNIGINER VPYNAPLIQF SSWMGGDRDG NPRVTPEVTR
DVCLLARMMA ANMYFSQIED LMFEMSMWRC TDELRVRAEE LFRTARRDVK HYIEFWKQVP
PTEPYRVILG DVRDKLYNTR ERARHLLAHD ISDIPEEAVY TNVEQFLEPL ELCYRSLCAC
GDRVIADGSL LDFLRQVSTF GLSLVKLDIR QESDRHTDVL DAITQHLEIG SYREWSEEKR
QEWLLAELSG KRPLFGSDLP KTEEIKDVLD TFNVLAELPS DCFGAYIISM ATSPSDVLAV
ELLQRECHVK QPLRVVPLFE KLADLEAAPA AMARLFSIDW YKNRINGKQE VMIGYSDSGK
DAGRFSAAWQ LYKAQEELKN VAKEFGVKLV MFHGRGGTVG RGGGPTHLAI LSQPPDTIQG
SLRVTVQGEV IEQSFGEEHL CFRTLQRFCA ATLEHGMNPP ISPRPEWREL MDQMAVVATE
QYRSIVFKEP RFVEYFRLAT PELEYGRMNI GSRPSKRKPS GGIESLRAIP WIFAWTQTRF
HLPVWLGFGA AFKQAIQKDS KNLQMLQEMY KTWPFFRVTI DLVEMVFAKG DPGIAALNDK
LLVSEDLWPF GESLRANYEE TKDYLLKIAG HKDLLEGDPY LKQRLKLRDS YITTLNVCQA
YTLKRTRDPN YHVTLRPHIS KEYAEPSKPA DELIHLNPTS EYAPGLEDTL ILTMKGIAAG
MQNTG
