SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P30694

- CAPPA_FLATR

UniProt

P30694 - CAPPA_FLATR

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

Functioni

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

Catalytic activityi

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-.UniRule annotation

Cofactori

Magnesium By similarity.UniRule annotation

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.UniRule annotation

Kineticsi

    Vmax=27 µmol/min/mg enzyme1 Publication

    Pathwayi

    Sites

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

    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 UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    Complete GO annotation...

    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 carboxylaseUniRule annotation
    PRO_0000166666Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei11 – 111Phosphoserine By 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

    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.

    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.UniRule annotation

    Sequence similaritiesi

    Belongs to the PEPCase type 1 family.

    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

    Sequence conflict

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

    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: April 16, 2014
    This is version 83 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

    Similar proteinsi