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P30694

- CAPPA_FLATR

UniProt

P30694 - CAPPA_FLATR

Protein

C4 phosphoenolpyruvate carboxylase

Gene

PPCA

Organism
Flaveria trinervia (Clustered yellowtops) (Oedera trinervia)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 84 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Forms oxaloacetate through the carboxylation of phosphoenolpyruvate (PEP). Catalyzes the first step of C4 photosynthesis.

    Catalytic activityi

    Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-.

    Cofactori

    Magnesium.By similarity

    Enzyme regulationi

    5 fold activation by the allosteric regulator glucose-6-phosphate. Low sensitivity to inhibition by L-malate. Up-regulated by light-reversible phosphorylation By similarity.By similarity

    Kineticsi

      Vmax=27 µmol/min/mg enzyme1 Publication

      Pathwayi

      Sites

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Active sitei172 – 1721By similarity
      Active sitei600 – 6001By similarity

      GO - Molecular functioni

      1. phosphoenolpyruvate carboxylase activity Source: UniProtKB

      GO - Biological processi

      1. C4 photosynthesis Source: UniProtKB
      2. carbon fixation Source: UniProtKB
      3. tricarboxylic acid cycle Source: InterPro

      Keywords - Molecular functioni

      Lyase

      Keywords - Biological processi

      Carbon dioxide fixation, Photosynthesis

      Keywords - Ligandi

      Magnesium

      Enzyme and pathway databases

      UniPathwayiUPA00322.

      Names & Taxonomyi

      Protein namesi
      Recommended name:
      C4 phosphoenolpyruvate carboxylase (EC:4.1.1.31)
      Short name:
      C4 PEPC
      Short name:
      C4 PEPCase
      Short name:
      ppcA
      Alternative name(s):
      Photosynthetic PEPCase
      Gene namesi
      Name:PPCA
      OrganismiFlaveria trinervia (Clustered yellowtops) (Oedera trinervia)
      Taxonomic identifieri4227 [NCBI]
      Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeAsteroideaeHeliantheae allianceTageteaeFlaveria

      Subcellular locationi

      Cytoplasm By similarity

      GO - Cellular componenti

      1. cytoplasm Source: UniProtKB-SubCell

      Keywords - Cellular componenti

      Cytoplasm

      Pathology & Biotechi

      Mutagenesis

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Mutagenesisi450 – 4501R → G: Loss of catalytic activity. 1 Publication
      Mutagenesisi600 – 6001K → R or T: Decreased bicarbonate-binding and lower catalytic activity. 1 Publication
      Mutagenesisi767 – 7671R → G: Loss of catalytic activity. 1 Publication
      Mutagenesisi774 – 7741S → A: Alteration of C4-specific kinetics, but no effect on L-malate tolerance. 2 Publications
      Mutagenesisi829 – 8291K → G: Decreased substrate binding and lower catalytic activity. 1 Publication

      PTM / Processingi

      Molecule processing

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Chaini1 – 966966C4 phosphoenolpyruvate carboxylasePRO_0000166666Add
      BLAST

      Amino acid modifications

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Modified residuei11 – 111PhosphoserineBy similarity

      Keywords - PTMi

      Phosphoprotein

      Expressioni

      Tissue specificityi

      Expressed in mesophyll cells, but not in bundle-sheath, roots, stems and flowers.2 Publications

      Interactioni

      Subunit structurei

      Homotetramer.

      Structurei

      Secondary structure

      1
      966
      Legend: HelixTurnBeta strand
      Show more details
      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Helixi9 – 1911
      Helixi30 – 4920
      Helixi51 – 7020
      Helixi73 – 8412
      Helixi88 – 11528
      Helixi126 – 1305
      Turni132 – 1343
      Helixi138 – 14811
      Helixi153 – 1619
      Beta strandi164 – 1696
      Helixi179 – 19517
      Helixi202 – 22019
      Helixi232 – 2398
      Helixi241 – 2455
      Helixi247 – 26317
      Turni264 – 2663
      Beta strandi278 – 2825
      Turni284 – 2863
      Helixi296 – 32429
      Helixi332 – 34312
      Helixi364 – 38926
      Helixi396 – 3983
      Helixi403 – 41917
      Helixi423 – 4264
      Helixi429 – 44012
      Beta strandi443 – 45210
      Helixi453 – 46614
      Turni472 – 4743
      Helixi477 – 48812
      Helixi503 – 51715
      Helixi520 – 5223
      Beta strandi523 – 5297
      Helixi534 – 54613
      Beta strandi555 – 5595
      Helixi562 – 57716
      Helixi579 – 5857
      Beta strandi588 – 5936
      Helixi595 – 6028
      Helixi604 – 62421
      Beta strandi628 – 6336
      Helixi638 – 6403
      Helixi644 – 6518
      Beta strandi661 – 6666
      Helixi668 – 6758
      Helixi678 – 69720
      Helixi705 – 72622
      Helixi732 – 7398
      Helixi742 – 7465
      Helixi762 – 7654
      Helixi768 – 77710
      Helixi782 – 7854
      Helixi788 – 79811
      Helixi801 – 81212
      Helixi814 – 82815
      Helixi832 – 84211
      Helixi845 – 8473
      Helixi848 – 86922
      Turni874 – 8774
      Helixi879 – 90729
      Helixi947 – 96216

      3D structure databases

      Select the link destinations:
      PDBe
      RCSB PDB
      PDBj
      Links Updated
      EntryMethodResolution (Å)ChainPositionsPDBsum
      3ZGEX-ray2.49A/B1-966[»]
      4BXCX-ray2.86A/B1-966[»]
      4BXHX-ray2.24A/B1-966[»]
      ProteinModelPortaliP30694.
      SMRiP30694. Positions 31-966.
      ModBaseiSearch...
      MobiDBiSearch...

      Family & Domainsi

      Domaini

      Region 2 (296-437) and region 5 (645-966) are involved in the acquisition of C4-specific properties. Region 5 (645-966) is involved in L-malate tolerance.

      Sequence similaritiesi

      Belongs to the PEPCase type 1 family.Curated

      Family and domain databases

      HAMAPiMF_00595. PEPcase_type1.
      InterProiIPR021135. PEP_COase.
      IPR018129. PEP_COase_AS.
      IPR022805. PEP_COase_bac/pln-type.
      IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
      [Graphical view]
      PfamiPF00311. PEPcase. 1 hit.
      [Graphical view]
      PRINTSiPR00150. PEPCARBXLASE.
      SUPFAMiSSF51621. SSF51621. 2 hits.
      PROSITEiPS00781. PEPCASE_1. 1 hit.
      PS00393. PEPCASE_2. 1 hit.
      [Graphical view]

      Sequencei

      Sequence statusi: Complete.

      P30694-1 [UniParc]FASTAAdd to Basket

      « Hide

      MANRNVEKLA SIDAQLRLLV PGKVSEDDKL VEYDALLLDK FLDILQDLHG    50
      EDLKEAVQQC YELSAEYEGK HDPKKLEELG SLLTSLDTGD SIVIAKAFSH 100
      MLNLANLAEE LQIAYRRRIK LKSGDFADEA NATTESDIEE TFKRLVHKLN 150
      KSPEEVFDAL KNQTVELVLT AHPTQSVRRS LLQKHGRIRN CLAQLYAKDI 200
      TPDDKQELDE ALHREIQAAF RTDEIRRTPP TPQDEMRAGM SYFHETIWKG 250
      VPKFLRRVDT ALKNIGINER FPYNAPLIQF SSWMGGDRDG NPRVTPEVTR 300
      DVCLLARMMT SNMYFSQIED LMIEMSMWRC NSELRVRAEE LYRTARKDVK 350
      HYIEFWKRIP PNQPYRVILG DVRDKLYNTR ERSRHLLVDG KSDIPDEAVY 400
      TNVEQLLEPL ELCYRSLCDC GDHVIADGSL LDFLRQVSTF GLSLVKLDIR 450
      QESDRHTEVL DAITQHLGIG SYREWSEEKR QEWLLAELSG KRPLIGPDLP 500
      KTEEVKDCLD TFKVLAELPS DCFGAYIISM ATSTSDVLAV ELLQREYHIK 550
      HPLRVVPLFE KLADLEAAPA AMTRLFSMDW YRNRIDGKQE VMIGYSDSGK 600
      DAGRFSAAWQ LYKTQEQIVK IAKEFGVKLV IFHGRGGTVG RGGGPTHLAL 650
      LSQPPDTING SLRVTVQGEV IEQSFGEEHL CFRTLQRFCA ATLEHGMNPP 700
      ISPRPEWREL MDQMAVVATE EYRSVVFKEP RFVEYFRLAT PELEFGRMNI 750
      GSRPSKRKPS GGIESLRAIP WIFSWTQTRF HLPVWLGFGA AFKHAIQKDS 800
      KNLQMLQEMY KTWPFFRVTI DLVEMVFAKG NPGIAALNDK LLVSEDLRPF 850
      GESLRANYEE TKNYLLKIAG HKDLLEGDPY LKQGIRLRDP YITTLNVCQA 900
      YTLKRIRDPN YHVTLRPHIS KEYAAEPSKP ADELIHLNPT SEYAPGLEDT 950
      LILTMKGIAA GMQNTG 966
      Length:966
      Mass (Da):110,406
      Last modified:February 1, 1996 - v2
      Checksum:i252F7B674BC94F47
      GO

      Experimental Info

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Sequence conflicti77 – 771E → D in CAA45504. (PubMed:1508152)Curated
      Sequence conflicti88 – 881T → P in CAA45504. (PubMed:1508152)Curated
      Sequence conflicti111 – 1111L → V in CAA45504. (PubMed:1508152)Curated
      Sequence conflicti177 – 1771V → I in CAA45504. (PubMed:1508152)Curated
      Sequence conflicti291 – 2911N → KH in CAA45504. (PubMed:1508152)Curated
      Sequence conflicti358 – 3581R → Q in CAA45504. (PubMed:1508152)Curated
      Sequence conflicti397 – 3971E → K in CAA81072. 1 PublicationCurated
      Sequence conflicti420 – 4201C → S in CAA45504. (PubMed:1508152)Curated
      Sequence conflicti513 – 5131K → N in CAA45504. (PubMed:1508152)Curated

      Sequence databases

      Select the link destinations:
      EMBL
      GenBank
      DDBJ
      Links Updated
      X61304 mRNA. Translation: CAA43601.1.
      X64143 Genomic DNA. Translation: CAA45504.1.
      Z25853 mRNA. Translation: CAA81072.1.
      PIRiS18318.
      S25082.
      S37072.

      Cross-referencesi

      Sequence databases

      Select the link destinations:
      EMBL
      GenBank
      DDBJ
      Links Updated
      X61304 mRNA. Translation: CAA43601.1 .
      X64143 Genomic DNA. Translation: CAA45504.1 .
      Z25853 mRNA. Translation: CAA81072.1 .
      PIRi S18318.
      S25082.
      S37072.

      3D structure databases

      Select the link destinations:
      PDBe
      RCSB PDB
      PDBj
      Links Updated
      Entry Method Resolution (Å) Chain Positions PDBsum
      3ZGE X-ray 2.49 A/B 1-966 [» ]
      4BXC X-ray 2.86 A/B 1-966 [» ]
      4BXH X-ray 2.24 A/B 1-966 [» ]
      ProteinModelPortali P30694.
      SMRi P30694. Positions 31-966.
      ModBasei Search...
      MobiDBi Search...

      Protocols and materials databases

      Structural Biology Knowledgebase Search...

      Enzyme and pathway databases

      UniPathwayi UPA00322 .

      Family and domain databases

      HAMAPi MF_00595. PEPcase_type1.
      InterProi IPR021135. PEP_COase.
      IPR018129. PEP_COase_AS.
      IPR022805. PEP_COase_bac/pln-type.
      IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
      [Graphical view ]
      Pfami PF00311. PEPcase. 1 hit.
      [Graphical view ]
      PRINTSi PR00150. PEPCARBXLASE.
      SUPFAMi SSF51621. SSF51621. 2 hits.
      PROSITEi PS00781. PEPCASE_1. 1 hit.
      PS00393. PEPCASE_2. 1 hit.
      [Graphical view ]
      ProtoNeti Search...

      Publicationsi

      1. "Multiple cDNAs of phosphoenolpyruvate carboxylase in the C4 dicot Flaveria trinervia."
        Poetsch W., Hermans J., Westhoff P.
        FEBS Lett. 292:133-136(1991) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
        Tissue: Leaf.
      2. Poetsch W.
        Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases
        Cited for: SEQUENCE REVISION.
      3. "Homologous genes for the C4 isoform of phosphoenolpyruvate carboxylase in a C3 and a C4 Flaveria species."
        Hermans J., Westhoff P.
        Mol. Gen. Genet. 234:275-284(1992) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      4. Bauwe H.
        Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
        Cited for: NUCLEOTIDE SEQUENCE [MRNA].
        Tissue: Leaf.
      5. "Site-directed mutagenesis of Lys600 in phosphoenolpyruvate carboxylase of Flaveria trinervia: its roles in catalytic and regulatory functions."
        Gao Y., Woo K.C.
        FEBS Lett. 375:95-98(1995) [PubMed] [Europe PMC] [Abstract]
        Cited for: MUTAGENESIS OF LYS-600.
      6. "Site-directed mutagenesis of Flaveria trinervia phosphoenolpyruvate carboxylase: Arg450 and Arg767 are essential for catalytic activity and Lys829 affects substrate binding."
        Gao Y., Woo K.C.
        FEBS Lett. 392:285-288(1996) [PubMed] [Europe PMC] [Abstract]
        Cited for: MUTAGENESIS OF ARG-450; ARG-767 AND LYS-829.
      7. "The phosphoenolpyruvate carboxylase (ppc) gene family of Flaveria trinervia (C4) and F. pringlei (C3): molecular characterization and expression analysis of the ppcB and ppcC genes."
        Ernst K., Westhoff P.
        Plant Mol. Biol. 34:427-443(1997) [PubMed] [Europe PMC] [Abstract]
        Cited for: TISSUE SPECIFICITY.
      8. "Evolution of C4 phosphoenolpyruvate carboxylase in Flaveria, a conserved serine residue in the carboxyl-terminal part of the enzyme is a major determinant for C4-specific characteristics."
        Blasing O.E., Westhoff P., Svensson P.
        J. Biol. Chem. 275:27917-27923(2000) [PubMed] [Europe PMC] [Abstract]
        Cited for: CHARACTERIZATION, MUTAGENESIS OF SER-774.
      9. "The non-photosynthetic phosphoenolpyruvate carboxylases of the C4 dicot Flaveria trinervia -- implications for the evolution of C4 photosynthesis."
        Blasing O.E., Ernst K., Streubel M., Westhoff P., Svensson P.
        Planta 215:448-456(2002) [PubMed] [Europe PMC] [Abstract]
        Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
      10. "Evolution of C(4) phosphoenolpyruvate carboxylase in Flaveria: determinants for high tolerance towards the inhibitor L-malate."
        Jacobs B., Engelmann S., Westhoff P., Gowik U.
        Plant Cell Environ. 31:793-803(2008) [PubMed] [Europe PMC] [Abstract]
        Cited for: CHARACTERIZATION, MUTAGENESIS OF SER-774.

      Entry informationi

      Entry nameiCAPPA_FLATR
      AccessioniPrimary (citable) accession number: P30694
      Secondary accession number(s): Q01648, Q42730
      Entry historyi
      Integrated into UniProtKB/Swiss-Prot: April 1, 1993
      Last sequence update: February 1, 1996
      Last modified: October 1, 2014
      This is version 84 of the entry and version 2 of the sequence. [Complete history]
      Entry statusiReviewed (UniProtKB/Swiss-Prot)
      Annotation programPlant Protein Annotation Program

      Miscellaneousi

      Miscellaneous

      Ser-774 is strongly involved in determining allosteric behavior of C4 PEPC.

      Keywords - Technical termi

      3D-structure, Allosteric enzyme

      Documents

      1. PATHWAY comments
        Index of metabolic and biosynthesis pathways
      2. PDB cross-references
        Index of Protein Data Bank (PDB) cross-references
      3. SIMILARITY comments
        Index of protein domains and families

      External Data

      Dasty 3