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Protein

C4 phosphoenolpyruvate carboxylase

Gene

PPCA

Organism
Flaveria trinervia (Clustered yellowtops) (Oedera trinervia)
Status
Reviewed-Annotation score: 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.

Catalytic activityi

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-.

Cofactori

Mg2+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

    1. Vmax=27 µmol/min/mg enzyme1 Publication

    Pathwayi: C4 acid pathway

    This protein is involved in the pathway C4 acid pathway, which is part of Photosynthesis.
    View all proteins of this organism that are known to be involved in the pathway C4 acid pathway and in Photosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei172By similarity1
    Active sitei600By similarity1

    GO - Molecular functioni

    • phosphoenolpyruvate carboxylase activity Source: UniProtKB

    GO - Biological processi

    • C4 photosynthesis Source: UniProtKB
    • carbon fixation Source: UniProtKB
    • 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

    BRENDAi4.1.1.31. 2270.
    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

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi450R → G: Loss of catalytic activity. 1 Publication1
    Mutagenesisi600K → R or T: Decreased bicarbonate-binding and lower catalytic activity. 1 Publication1
    Mutagenesisi767R → G: Loss of catalytic activity. 1 Publication1
    Mutagenesisi774S → A: Alteration of C4-specific kinetics, but no effect on L-malate tolerance. 2 Publications1
    Mutagenesisi829K → G: Decreased substrate binding and lower catalytic activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001666661 – 966C4 phosphoenolpyruvate carboxylaseAdd BLAST966

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei11PhosphoserineBy similarity1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP30694.

    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

    1966
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi9 – 19Combined sources11
    Helixi30 – 49Combined sources20
    Helixi51 – 70Combined sources20
    Helixi73 – 84Combined sources12
    Helixi88 – 115Combined sources28
    Helixi126 – 130Combined sources5
    Turni132 – 134Combined sources3
    Helixi138 – 148Combined sources11
    Helixi153 – 161Combined sources9
    Beta strandi164 – 169Combined sources6
    Helixi179 – 195Combined sources17
    Helixi202 – 220Combined sources19
    Helixi232 – 239Combined sources8
    Helixi241 – 245Combined sources5
    Helixi247 – 263Combined sources17
    Turni264 – 266Combined sources3
    Beta strandi278 – 282Combined sources5
    Turni284 – 286Combined sources3
    Helixi296 – 324Combined sources29
    Helixi332 – 343Combined sources12
    Helixi364 – 389Combined sources26
    Helixi396 – 398Combined sources3
    Helixi403 – 419Combined sources17
    Helixi423 – 426Combined sources4
    Helixi429 – 440Combined sources12
    Beta strandi443 – 452Combined sources10
    Helixi453 – 466Combined sources14
    Turni472 – 474Combined sources3
    Helixi477 – 488Combined sources12
    Helixi503 – 517Combined sources15
    Helixi520 – 522Combined sources3
    Beta strandi523 – 529Combined sources7
    Helixi534 – 546Combined sources13
    Beta strandi555 – 559Combined sources5
    Helixi562 – 577Combined sources16
    Helixi579 – 585Combined sources7
    Beta strandi588 – 593Combined sources6
    Helixi595 – 602Combined sources8
    Helixi604 – 624Combined sources21
    Beta strandi628 – 633Combined sources6
    Helixi638 – 640Combined sources3
    Helixi644 – 651Combined sources8
    Beta strandi661 – 666Combined sources6
    Helixi668 – 675Combined sources8
    Helixi678 – 697Combined sources20
    Helixi705 – 726Combined sources22
    Helixi732 – 739Combined sources8
    Helixi742 – 746Combined sources5
    Helixi762 – 765Combined sources4
    Helixi768 – 777Combined sources10
    Helixi782 – 785Combined sources4
    Helixi788 – 798Combined sources11
    Helixi801 – 812Combined sources12
    Helixi814 – 828Combined sources15
    Helixi832 – 842Combined sources11
    Helixi845 – 847Combined sources3
    Helixi848 – 869Combined sources22
    Turni874 – 877Combined sources4
    Helixi879 – 907Combined sources29
    Helixi947 – 962Combined sources16

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3ZGEX-ray2.49A/B1-966[»]
    4BXCX-ray2.86A/B1-966[»]
    4BXHX-ray2.24A/B1-966[»]
    ProteinModelPortaliP30694.
    SMRiP30694.
    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. 1 hit.
    InterProiIPR021135. PEP_COase.
    IPR022805. PEP_COase_bac/pln-type.
    IPR018129. PEP_COase_Lys_AS.
    IPR033129. PEPCASE_His_AS.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view]
    PfamiPF00311. PEPcase. 1 hit.
    [Graphical view]
    PRINTSiPR00150. PEPCARBXLASE.
    SUPFAMiSSF51621. SSF51621. 1 hit.
    PROSITEiPS00781. PEPCASE_1. 1 hit.
    PS00393. PEPCASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P30694-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MANRNVEKLA SIDAQLRLLV PGKVSEDDKL VEYDALLLDK FLDILQDLHG
    60 70 80 90 100
    EDLKEAVQQC YELSAEYEGK HDPKKLEELG SLLTSLDTGD SIVIAKAFSH
    110 120 130 140 150
    MLNLANLAEE LQIAYRRRIK LKSGDFADEA NATTESDIEE TFKRLVHKLN
    160 170 180 190 200
    KSPEEVFDAL KNQTVELVLT AHPTQSVRRS LLQKHGRIRN CLAQLYAKDI
    210 220 230 240 250
    TPDDKQELDE ALHREIQAAF RTDEIRRTPP TPQDEMRAGM SYFHETIWKG
    260 270 280 290 300
    VPKFLRRVDT ALKNIGINER FPYNAPLIQF SSWMGGDRDG NPRVTPEVTR
    310 320 330 340 350
    DVCLLARMMT SNMYFSQIED LMIEMSMWRC NSELRVRAEE LYRTARKDVK
    360 370 380 390 400
    HYIEFWKRIP PNQPYRVILG DVRDKLYNTR ERSRHLLVDG KSDIPDEAVY
    410 420 430 440 450
    TNVEQLLEPL ELCYRSLCDC GDHVIADGSL LDFLRQVSTF GLSLVKLDIR
    460 470 480 490 500
    QESDRHTEVL DAITQHLGIG SYREWSEEKR QEWLLAELSG KRPLIGPDLP
    510 520 530 540 550
    KTEEVKDCLD TFKVLAELPS DCFGAYIISM ATSTSDVLAV ELLQREYHIK
    560 570 580 590 600
    HPLRVVPLFE KLADLEAAPA AMTRLFSMDW YRNRIDGKQE VMIGYSDSGK
    610 620 630 640 650
    DAGRFSAAWQ LYKTQEQIVK IAKEFGVKLV IFHGRGGTVG RGGGPTHLAL
    660 670 680 690 700
    LSQPPDTING SLRVTVQGEV IEQSFGEEHL CFRTLQRFCA ATLEHGMNPP
    710 720 730 740 750
    ISPRPEWREL MDQMAVVATE EYRSVVFKEP RFVEYFRLAT PELEFGRMNI
    760 770 780 790 800
    GSRPSKRKPS GGIESLRAIP WIFSWTQTRF HLPVWLGFGA AFKHAIQKDS
    810 820 830 840 850
    KNLQMLQEMY KTWPFFRVTI DLVEMVFAKG NPGIAALNDK LLVSEDLRPF
    860 870 880 890 900
    GESLRANYEE TKNYLLKIAG HKDLLEGDPY LKQGIRLRDP YITTLNVCQA
    910 920 930 940 950
    YTLKRIRDPN YHVTLRPHIS KEYAAEPSKP ADELIHLNPT SEYAPGLEDT
    960
    LILTMKGIAA GMQNTG
    Length:966
    Mass (Da):110,406
    Last modified:February 1, 1996 - v2
    Checksum:i252F7B674BC94F47
    GO

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sequence conflicti77E → D in CAA45504 (PubMed:1508152).Curated1
    Sequence conflicti88T → P in CAA45504 (PubMed:1508152).Curated1
    Sequence conflicti111L → V in CAA45504 (PubMed:1508152).Curated1
    Sequence conflicti177V → I in CAA45504 (PubMed:1508152).Curated1
    Sequence conflicti291N → KH in CAA45504 (PubMed:1508152).Curated1
    Sequence conflicti358R → Q in CAA45504 (PubMed:1508152).Curated1
    Sequence conflicti397E → K in CAA81072 (Ref. 4) Curated1
    Sequence conflicti420C → S in CAA45504 (PubMed:1508152).Curated1
    Sequence conflicti513K → N in CAA45504 (PubMed:1508152).Curated1

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    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:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X61304 mRNA. Translation: CAA43601.1.
    X64143 Genomic DNA. Translation: CAA45504.1.
    Z25853 mRNA. Translation: CAA81072.1.
    PIRiS18318.
    S25082.
    S37072.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    3ZGEX-ray2.49A/B1-966[»]
    4BXCX-ray2.86A/B1-966[»]
    4BXHX-ray2.24A/B1-966[»]
    ProteinModelPortaliP30694.
    SMRiP30694.
    ModBaseiSearch...
    MobiDBiSearch...

    Proteomic databases

    PRIDEiP30694.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    UniPathwayiUPA00322.
    BRENDAi4.1.1.31. 2270.

    Family and domain databases

    HAMAPiMF_00595. PEPcase_type1. 1 hit.
    InterProiIPR021135. PEP_COase.
    IPR022805. PEP_COase_bac/pln-type.
    IPR018129. PEP_COase_Lys_AS.
    IPR033129. PEPCASE_His_AS.
    IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
    [Graphical view]
    PfamiPF00311. PEPcase. 1 hit.
    [Graphical view]
    PRINTSiPR00150. PEPCARBXLASE.
    SUPFAMiSSF51621. SSF51621. 1 hit.
    PROSITEiPS00781. PEPCASE_1. 1 hit.
    PS00393. PEPCASE_2. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    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: November 30, 2016
    This is version 96 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.