Skip Header

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

Phosphoenolpyruvate carboxylase 2

Gene

PPCC

Organism
Flaveria trinervia (Clustered yellowtops) (Oedera trinervia)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Through the carboxylation of phosphoenolpyruvate (PEP) it forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.

Catalytic activityi

Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-.

Cofactori

Mg2+By similarity

Enzyme regulationi

Inhibited by malate. Up regulated by light-reversible phosphorylation (By similarity).By similarity

Kineticsi

    1. Vmax=59 µmol/min/mg enzyme1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei172By similarity1
    Active sitei601By similarity1

    GO - Molecular functioni

    • phosphoenolpyruvate carboxylase activity Source: UniProtKB

    GO - Biological processi

    • carbon fixation Source: UniProtKB
    • tricarboxylic acid cycle Source: InterPro
    Complete GO annotation...

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Carbon dioxide fixation

    Keywords - Ligandi

    Magnesium

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoenolpyruvate carboxylase 2 (EC:4.1.1.31)
    Short name:
    PEPC 2
    Short name:
    PEPCase 2
    Short name:
    ppcC
    Gene namesi
    Name:PPCC
    OrganismiFlaveria trinervia (Clustered yellowtops) (Oedera trinervia)
    Taxonomic identifieri4227 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeAsteroideaeHeliantheae allianceTageteaeFlaveria

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00004034401 – 967Phosphoenolpyruvate carboxylase 2Add BLAST967

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei11PhosphoserineBy similarity1

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ9FV65.

    Expressioni

    Tissue specificityi

    Expressed in roots and stems and at low levels in leaves.1 Publication

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9FV65.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    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.

    Q9FV65-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MANRNLEKLA SIDAQLRLLV PGKVSEDDKL IEYDALLLDK FLDILQDLHG
    60 70 80 90 100
    EGLKETVQEC YELSAEYEGK HDPKKLEELG NVLTSLDPGD SIVIAKAFSH
    110 120 130 140 150
    MLNLANLAEE VQIAYRRRIK LKKGDFADEA SATTESDIEE TFKKLVHKLK
    160 170 180 190 200
    KSPEEVFDAL KNQTVDLVFT AHPTQSVRRS LLQKHGRIRD CLAQLYAKDI
    210 220 230 240 250
    TPDDKQELDE ALHREIQAAF RTDEIRRTPP TPQDEMRAGM SYFHETIWKG
    260 270 280 290 300
    VPKFLRRVDT ALKNIGINER VPYNAPLIQF SSWMGGDRDG NPRVTPEVTR
    310 320 330 340 350
    DVCLLARMMA ANMYFSQIED LMFEMSMWRC SDELRVRAEE LHRSSSKRDV
    360 370 380 390 400
    KHYIEFWKQV PPTEPYRVIL GDVRDKLYNT RERARHLLAH DVSDIPEESV
    410 420 430 440 450
    YTNVEQFLEP LELCYRSLCA CGDRVIADGS LLDFLRQVST FGLSLVRLDI
    460 470 480 490 500
    RQESDRHTDV LDAITQHLEI GSYREWSEEK RQEWLLSELS GKRPLFGPDL
    510 520 530 540 550
    PKTEEIADVL DTFHVLAELP ADCFGAYIIS MATSPSDVLA VELLQRECHV
    560 570 580 590 600
    KQPLRVVPLF EKLADLEAAP AAVARLFSIE WYKNRIDGKQ EVMIGYSDSG
    610 620 630 640 650
    KDAGRLSAAW QLYKAQEELI NVAKKFGVKL TMFHGRGGTV GRGGGPTHLA
    660 670 680 690 700
    ILSQPPETIH GSLRVTVQGE VIEQSFGEEH LCFRTLQRFC AATLEHGMNP
    710 720 730 740 750
    PISPRPEWRA LMDEMAVYAT EQYREIVFKE PRFVEYFRLA TPELEYGRMN
    760 770 780 790 800
    IGSRPSKRKP SGGIESLRAI PWIFAWTQTR FHLPVWLGFG AAFKYAIEKD
    810 820 830 840 850
    IKNLHMLQEM YKTWPFFRVT IDLVEMVFAK GDPGIAALND KLLVSEDLWS
    860 870 880 890 900
    FGESLRANYE ETKNLLLKIA GHKDLLEGDP YLRQRLRLRD SYITTLNVCQ
    910 920 930 940 950
    AYTLKRIRDP NYHVTFRPHI SKEYSEPSSK PADEYIKLNP KSEYAPGLED
    960
    TLILTMKGIA AGMQNTG
    Length:967
    Mass (Da):110,646
    Last modified:March 1, 2001 - v1
    Checksum:i68093CB5CB370D37
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF248080 mRNA. Translation: AAG17619.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF248080 mRNA. Translation: AAG17619.1.

    3D structure databases

    ProteinModelPortaliQ9FV65.
    ModBaseiSearch...
    MobiDBiSearch...

    Proteomic databases

    PRIDEiQ9FV65.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    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 nameiCAPPC_FLATR
    AccessioniPrimary (citable) accession number: Q9FV65
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 11, 2011
    Last sequence update: March 1, 2001
    Last modified: November 30, 2016
    This is version 59 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Documents

    1. 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.