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Q01647

- CAPP1_FLAPR

UniProt

Q01647 - CAPP1_FLAPR

Protein

Phosphoenolpyruvate carboxylase

Gene

PPCA1

Organism
Flaveria pringlei
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 80 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
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    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

    Magnesium.By similarity

    Enzyme regulationi

    By light-reversible phosphorylation.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei172 – 1721By similarity
    Active sitei601 – 6011By similarity

    GO - Molecular functioni

    1. phosphoenolpyruvate carboxylase activity Source: UniProtKB-EC

    GO - Biological processi

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

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Carbon dioxide fixation, Photosynthesis

    Keywords - Ligandi

    Magnesium

    Enzyme and pathway databases

    UniPathwayiUPA00321.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoenolpyruvate carboxylase (EC:4.1.1.31)
    Short name:
    PEPC
    Short name:
    PEPCase
    Gene namesi
    Name:PPCA1
    OrganismiFlaveria pringlei
    Taxonomic identifieri4226 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeAsteroideaeHeliantheae allianceTageteaeFlaveria

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 967967Phosphoenolpyruvate carboxylasePRO_0000166664Add
    BLAST

    Amino acid modifications

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

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ01647.

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    Secondary structure

    1
    967
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 1911
    Helixi30 – 4920
    Helixi51 – 7020
    Helixi74 – 8310
    Helixi88 – 11528
    Helixi126 – 1305
    Turni132 – 1343
    Helixi138 – 14811
    Helixi153 – 1619
    Beta strandi164 – 1696
    Helixi179 – 19517
    Helixi202 – 22019
    Helixi232 – 2398
    Helixi242 – 2454
    Helixi247 – 26418
    Beta strandi278 – 2825
    Turni284 – 2863
    Helixi297 – 32529
    Helixi333 – 34412
    Helixi365 – 39026
    Helixi397 – 3993
    Helixi404 – 42017
    Helixi424 – 4274
    Helixi430 – 44112
    Beta strandi444 – 45310
    Helixi454 – 46714
    Turni473 – 4753
    Helixi478 – 48912
    Helixi504 – 51815
    Helixi521 – 5233
    Beta strandi524 – 5307
    Helixi535 – 54713
    Beta strandi555 – 5606
    Helixi563 – 57715
    Helixi580 – 5867
    Beta strandi589 – 5946
    Helixi596 – 6038
    Helixi605 – 62622
    Beta strandi629 – 6346
    Helixi639 – 6413
    Helixi645 – 6528
    Beta strandi662 – 6676
    Turni669 – 6713
    Helixi672 – 6765
    Helixi679 – 69820
    Helixi706 – 72722
    Helixi733 – 7408
    Helixi743 – 7486
    Beta strandi751 – 7533
    Turni764 – 7663
    Helixi769 – 7779
    Turni778 – 7803
    Helixi783 – 7864
    Helixi789 – 79911
    Helixi802 – 81312
    Helixi815 – 82915
    Helixi833 – 84311
    Helixi846 – 8483
    Helixi849 – 87022
    Turni875 – 8784
    Helixi880 – 90829
    Helixi948 – 96316

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3ZGBX-ray2.71A/B6-967[»]
    ProteinModelPortaliQ01647.
    SMRiQ01647. Positions 31-967.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    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.

    Q01647-1 [UniParc]FASTAAdd to Basket

    « Hide

    MANRNLEKLA SIDAQLRLLV PGKVSEDDKL IEYDALLLDK FLDILQDLHG    50
    EDLKEAVQEC YELSAEYEGK HDPKKLEELG SVLTSLDPGD SIVIAKAFSH 100
    MLNLANLAEE VQIAYRRRIK LKRGDFADEA NATTESDIEE TFKKLVLKLN 150
    KSPEEVFDAL KNQTVDLVLT AHPTQSVRRS LLQKHGRIRN CLAQLYAKDI 200
    TPDDKQELDE ALHREIQAAF RTDEIRRTPP TPQDEMRAGM SYFHETIWKG 250
    VPKFLRRVDT ALKNIGINER VPYNAPLIQF SSWMGGDRDG KHPRVTPEVT 300
    RDVCLLARMM ASNMYFSQIE DLMFEMSMWR CNSELRVRAE ELYRTARRDV 350
    KHYIEFWKQV PPTEPYRVIL GDVRDKLYNT RERSRHLLAH GISDIPEEAV 400
    YTNVEQFLEP LELCYRSLCD CGDRVIADGS LLDFLRQVST FGLSLVKLDI 450
    RQESDRHTDV LDAITQHLEI GSYREWSEEK RQEWLLAELS GKRPLFGSDL 500
    PKTEEVKDVL DTFNVLAELP SDCFGAYIIS MATSPSDVLA VELLQRECHV 550
    KHPLRVVPLF EKLADLEAAP AAMARLFSID WYRNRIDGKQ EVMIGYSDSG 600
    KDAGRFSAAW QLYKAQEEII KVAKEFGVKL VIFHGRGGTV GRGGGPTHLA 650
    ILSQPPDTIH GSLRVTVQGE VIEQSFGEEH LCFRTLQRFC AATLEHGMNP 700
    PISPRPEWRE LMDQMAVVAT EEYRSIVFKE PRFVEYFRLA TPELEYGRMN 750
    IGSRPSKRKP SGGIESLRAI PWIFAWTQTR FHLPVWLGFG AAFKHAIKKD 800
    SKNLQMLQEM YKTWPFFRVT IDLVEMVFAK GDPGIAALND KLLVSEDLWP 850
    FGESLRANYE ETKDYLLKIA GHRDLLEGDP YLKQRIRLRD SYITTLNVCQ 900
    AYTLKRIRDP NYHVTLRPHI SKEYAAEPSK PADELIHLNP TSEYAPGLED 950
    TLILTMKGIA AGMQNTG 967
    Length:967
    Mass (Da):110,629
    Last modified:April 1, 1993 - v1
    Checksum:i8317EA8078C038C0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti291 – 2922KH → N in CAA88829. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64144 Genomic DNA. Translation: CAA45505.1.
    Z48966 mRNA. Translation: CAA88829.1.
    PIRiS25081.
    S52853.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X64144 Genomic DNA. Translation: CAA45505.1 .
    Z48966 mRNA. Translation: CAA88829.1 .
    PIRi S25081.
    S52853.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3ZGB X-ray 2.71 A/B 6-967 [» ]
    ProteinModelPortali Q01647.
    SMRi Q01647. Positions 31-967.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q01647.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00321 .

    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. "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].
    2. Svensson P., Blaesing O.E., Westhoff P.
      Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Leaf.

    Entry informationi

    Entry nameiCAPP1_FLAPR
    AccessioniPrimary (citable) accession number: Q01647
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 80 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    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