CAPPC_FLATR
ID CAPPC_FLATR Reviewed; 967 AA.
AC Q9FV65;
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 2 {ECO:0000303|PubMed:12111227};
DE Short=PEPC 2 {ECO:0000303|PubMed:12111227};
DE Short=PEPCase 2 {ECO:0000303|PubMed:12111227};
DE Short=ppcC {ECO:0000303|PubMed:9225854};
DE EC=4.1.1.31 {ECO:0000269|PubMed:12111227};
GN Name=PPCC {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], BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, FUNCTION, 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.
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. {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=59 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. {ECO:0000269|PubMed:9225854}.
CC -!- SIMILARITY: Belongs to the PEPCase type 1 family. {ECO:0000305}.
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DR EMBL; AF248080; AAG17619.1; -; mRNA.
DR AlphaFoldDB; Q9FV65; -.
DR SMR; Q9FV65; -.
DR PRIDE; Q9FV65; -.
DR SABIO-RK; Q9FV65; -.
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: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..967
FT /note="Phosphoenolpyruvate carboxylase 2"
FT /id="PRO_0000403440"
FT ACT_SITE 172
FT /evidence="ECO:0000250|UniProtKB:P04711"
FT ACT_SITE 601
FT /evidence="ECO:0000250|UniProtKB:P04711"
FT ACT_SITE 642
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 451
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 598
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 636
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 642
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 666
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 674
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 754
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 768..770
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 830
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 889
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P30694"
FT BINDING 965
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 967 AA; 110646 MW; 68093CB5CB370D37 CRC64;
MANRNLEKLA SIDAQLRLLV PGKVSEDDKL IEYDALLLDK FLDILQDLHG EGLKETVQEC
YELSAEYEGK HDPKKLEELG NVLTSLDPGD SIVIAKAFSH MLNLANLAEE VQIAYRRRIK
LKKGDFADEA SATTESDIEE TFKKLVHKLK KSPEEVFDAL KNQTVDLVFT AHPTQSVRRS
LLQKHGRIRD CLAQLYAKDI TPDDKQELDE ALHREIQAAF RTDEIRRTPP TPQDEMRAGM
SYFHETIWKG VPKFLRRVDT ALKNIGINER VPYNAPLIQF SSWMGGDRDG NPRVTPEVTR
DVCLLARMMA ANMYFSQIED LMFEMSMWRC SDELRVRAEE LHRSSSKRDV KHYIEFWKQV
PPTEPYRVIL GDVRDKLYNT RERARHLLAH DVSDIPEESV YTNVEQFLEP LELCYRSLCA
CGDRVIADGS LLDFLRQVST FGLSLVRLDI RQESDRHTDV LDAITQHLEI GSYREWSEEK
RQEWLLSELS GKRPLFGPDL PKTEEIADVL DTFHVLAELP ADCFGAYIIS MATSPSDVLA
VELLQRECHV KQPLRVVPLF EKLADLEAAP AAVARLFSIE WYKNRIDGKQ EVMIGYSDSG
KDAGRLSAAW QLYKAQEELI NVAKKFGVKL TMFHGRGGTV GRGGGPTHLA ILSQPPETIH
GSLRVTVQGE VIEQSFGEEH LCFRTLQRFC AATLEHGMNP PISPRPEWRA LMDEMAVYAT
EQYREIVFKE PRFVEYFRLA TPELEYGRMN IGSRPSKRKP SGGIESLRAI PWIFAWTQTR
FHLPVWLGFG AAFKYAIEKD IKNLHMLQEM YKTWPFFRVT IDLVEMVFAK GDPGIAALND
KLLVSEDLWS FGESLRANYE ETKNLLLKIA GHKDLLEGDP YLRQRLRLRD SYITTLNVCQ
AYTLKRIRDP NYHVTFRPHI SKEYSEPSSK PADEYIKLNP KSEYAPGLED TLILTMKGIA
AGMQNTG
