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P04711

- CAPP1_MAIZE

UniProt

P04711 - CAPP1_MAIZE

Protein

Phosphoenolpyruvate carboxylase 1

Gene

PEP1

Organism
Zea mays (Maize)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (01 Oct 1989)
      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 sitei177 – 17711 Publication
    Active sitei606 – 60611 Publication
    Active sitei647 – 64711 Publication

    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

    SABIO-RKP04711.
    UniPathwayiUPA00322.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoenolpyruvate carboxylase 1 (EC:4.1.1.31)
    Short name:
    PEPC 1
    Short name:
    PEPCase 1
    Gene namesi
    Name:PEP1
    Synonyms:PPC
    OrganismiZea mays (Maize)
    Taxonomic identifieri4577 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

    Organism-specific databases

    GrameneiP04711.
    MaizeGDBi30066.

    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 – 970970Phosphoenolpyruvate carboxylase 1PRO_0000166667Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei15 – 151Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP04711.

    Interactioni

    Subunit structurei

    Homotetramer.

    Structurei

    Secondary structure

    1
    970
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi36 – 5318
    Helixi55 – 7218
    Helixi78 – 8912
    Helixi92 – 12231
    Helixi143 – 1519
    Helixi158 – 1669
    Beta strandi169 – 1757
    Helixi184 – 19916
    Helixi207 – 22620
    Helixi237 – 24812
    Turni249 – 2557
    Helixi256 – 26813
    Turni269 – 2713
    Beta strandi282 – 2876
    Turni289 – 2913
    Helixi301 – 32929
    Helixi337 – 35014
    Beta strandi359 – 3613
    Helixi370 – 39425
    Helixi409 – 42517
    Turni430 – 4345
    Helixi435 – 44612
    Beta strandi449 – 4568
    Helixi459 – 47315
    Helixi483 – 49513
    Helixi509 – 52315
    Beta strandi529 – 5346
    Helixi541 – 55212
    Beta strandi561 – 5655
    Helixi568 – 5725
    Helixi574 – 5829
    Helixi585 – 5917
    Beta strandi593 – 6019
    Helixi604 – 6074
    Helixi610 – 62920
    Turni630 – 6323
    Beta strandi634 – 6407
    Helixi645 – 6473
    Helixi652 – 6576
    Beta strandi667 – 6737
    Helixi674 – 6818
    Helixi684 – 70320
    Helixi711 – 73222
    Helixi738 – 7458
    Helixi749 – 7546
    Helixi775 – 7839
    Helixi788 – 7914
    Helixi794 – 80411
    Helixi808 – 81811
    Helixi820 – 83314
    Helixi838 – 84710
    Helixi854 – 87522
    Helixi885 – 91329
    Turni937 – 9415
    Beta strandi942 – 9443
    Helixi951 – 96616

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JQOX-ray3.00A/B1-970[»]
    ProteinModelPortaliP04711.
    SMRiP04711. Positions 35-970.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP04711.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the PEPCase type 1 family.Curated

    Phylogenomic databases

    HOGENOMiHOG000238648.
    KOiK01595.

    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. 1 hit.
    PROSITEiPS00781. PEPCASE_1. 1 hit.
    PS00393. PEPCASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P04711-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASTKAPGPG EKHHSIDAQL RQLVPGKVSE DDKLIEYDAL LVDRFLNILQ    50
    DLHGPSLREF VQECYEVSAD YEGKGDTTKL GELGAKLTGL APADAILVAS 100
    SILHMLNLAN LAEEVQIAHR RRNSKLKKGG FADEGSATTE SDIEETLKRL 150
    VSEVGKSPEE VFEALKNQTV DLVFTAHPTQ SARRSLLQKN ARIRNCLTQL 200
    NAKDITDDDK QELDEALQRE IQAAFRTDEI RRAQPTPQAE MRYGMSYIHE 250
    TVWKGVPKFL RRVDTALKNI GINERLPYNV SLIRFSSWMG GDRDGNPRVT 300
    PEVTRDVCLL ARMMAANLYI DQIEELMFEL SMWRCNDELR VRAEELHSSS 350
    GSKVTKYYIE FWKQIPPNEP YRVILGHVRD KLYNTRERAR HLLASGVSEI 400
    SAESSFTSIE EFLEPLELCY KSLCDCGDKA IADGSLLDLL RQVFTFGLSL 450
    VKLDIRQESE RHTDVIDAIT THLGIGSYRE WPEDKRQEWL LSELRGKRPL 500
    LPPDLPQTDE IADVIGAFHV LAELPPDSFG PYIISMATAP SDVLAVELLQ 550
    RECGVRQPLP VVPLFERLAD LQSAPASVER LFSVDWYMDR IKGKQQVMVG 600
    YSDSGKDAGR LSAAWQLYRA QEEMAQVAKR YGVKLTLFHG RGGTVGRGGG 650
    PTHLAILSQP PDTINGSIRV TVQGEVIEFC FGEEHLCFQT LQRFTAATLE 700
    HGMHPPVSPK PEWRKLMDEM AVVATEEYRS VVVKEARFVE YFRSATPETE 750
    YGRMNIGSRP AKRRPGGGIT TLRAIPWIFS WTQTRFHLPV WLGVGAAFKF 800
    AIDKDVRNFQ VLKEMYNEWP FFRVTLDLLE MVFAKGDPGI AGLYDELLVA 850
    EELKPFGKQL RDKYVETQQL LLQIAGHKDI LEGDPFLKQG LVLRNPYITT 900
    LNVFQAYTLK RIRDPNFKVT PQPPLSKEFA DENKPAGLVK LNPASEYPPG 950
    LEDTLILTMK GIAAGMQNTG 970
    Length:970
    Mass (Da):109,297
    Last modified:October 1, 1989 - v2
    Checksum:i95B66F96ABCE22F4
    GO

    Sequence cautioni

    The sequence CAA32722.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti239 – 2391A → D(PubMed:3005978)Curated
    Sequence conflicti239 – 2391A → D(PubMed:2731539)Curated
    Sequence conflicti338 – 3392EL → DV in CAA27270. (PubMed:3005978)Curated
    Sequence conflicti482 – 4821P → S(PubMed:3005978)Curated
    Sequence conflicti482 – 4821P → S(PubMed:2731539)Curated
    Sequence conflicti509 – 5091D → E in CAA33663. (PubMed:2731539)Curated
    Sequence conflicti557 – 5593QPL → PAV(PubMed:3005978)Curated
    Sequence conflicti557 – 5593QPL → PAV(PubMed:2731539)Curated
    Sequence conflicti570 – 5701D → S(PubMed:3005978)Curated
    Sequence conflicti570 – 5701D → S(PubMed:2731539)Curated
    Sequence conflicti573 – 5742SA → LR in CAA27270. (PubMed:3005978)Curated
    Sequence conflicti687 – 6871C → S in CAA27270. (PubMed:3005978)Curated
    Sequence conflicti736 – 7361A → P in CAA27270. (PubMed:3005978)Curated
    Sequence conflicti963 – 9631A → R in CAA27270. (PubMed:3005978)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15238 mRNA. Translation: CAA33316.1.
    X03613 mRNA. Translation: CAA27270.1.
    X14581 Genomic DNA. Translation: CAA32724.1.
    X14579 Genomic DNA. Translation: CAA32722.1. Different initiation.
    X14580 Genomic DNA. Translation: CAA32723.1.
    X15642 Genomic DNA. Translation: CAA33663.1.
    X07168 mRNA. Translation: CAA30158.1.
    RefSeqiNP_001105418.1. NM_001111948.1.
    UniGeneiZm.2433.

    Genome annotation databases

    GeneIDi542372.
    KEGGizma:542372.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15238 mRNA. Translation: CAA33316.1 .
    X03613 mRNA. Translation: CAA27270.1 .
    X14581 Genomic DNA. Translation: CAA32724.1 .
    X14579 Genomic DNA. Translation: CAA32722.1 . Different initiation.
    X14580 Genomic DNA. Translation: CAA32723.1 .
    X15642 Genomic DNA. Translation: CAA33663.1 .
    X07168 mRNA. Translation: CAA30158.1 .
    RefSeqi NP_001105418.1. NM_001111948.1.
    UniGenei Zm.2433.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JQO X-ray 3.00 A/B 1-970 [» ]
    ProteinModelPortali P04711.
    SMRi P04711. Positions 35-970.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi P04711.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 542372.
    KEGGi zma:542372.

    Organism-specific databases

    Gramenei P04711.
    MaizeGDBi 30066.

    Phylogenomic databases

    HOGENOMi HOG000238648.
    KOi K01595.

    Enzyme and pathway databases

    UniPathwayi UPA00322 .
    SABIO-RK P04711.

    Miscellaneous databases

    EvolutionaryTracei P04711.

    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. 1 hit.
    PROSITEi PS00781. PEPCASE_1. 1 hit.
    PS00393. PEPCASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure and expression of the maize gene encoding the phosphoenolpyruvate carboxylase isozyme involved in C4 photosynthesis."
      Hudspeth R.L., Grula J.W.
      Plant Mol. Biol. 12:579-589(1989)
      Cited for: NUCLEOTIDE SEQUENCE.
      Strain: cv. B73.
      Tissue: Leaf.
    2. "Cloning and sequence analysis of cDNA encoding active phosphoenolpyruvate carboxylase of the C4-pathway from maize."
      Izui K., Ishijima S., Yamaguchi Y., Katagiri F., Murata T., Shigesada K., Sugiyama T., Katsuki H.
      Nucleic Acids Res. 14:1615-1628(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 39-970.
    3. "Complete structure of the gene for phosphoenolpyruvate carboxylase from maize."
      Matsuoka M., Minami E.
      Eur. J. Biochem. 181:593-598(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Golden cross Bantam.
    4. "Maize phosphoenolpyruvate carboxylase involved in C4 photosynthesis: nucleotide sequence analysis of the 5' flanking region of the gene."
      Yanagisawa S., Izui K.
      J. Biochem. 106:982-987(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-3.
      Strain: cv. H84.
      Tissue: Leaf.
    5. "Further analysis of cDNA clones for maize phosphoenolpyruvate carboxylase involved in C4 photosynthesis. Nucleotide sequence of entire open reading frame and evidence for polyadenylation of mRNA at multiple sites in vivo."
      Yanagisawa S., Izui K., Yamaguchi Y., Shigesada K., Katsuki H.
      FEBS Lett. 229:107-110(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-82.
    6. "Isolation and sequence of an active-site peptide from maize leaf phosphoenolpyruvate carboxylase inactivated by pyridoxal 5'-phosphate."
      Jiao J.-A., Podesta F.E., Chollet R., O'Leary M.H., Andreo C.S.
      Biochim. Biophys. Acta 1041:291-295(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE, PROTEIN SEQUENCE OF 599-610.
    7. "In vivo regulatory phosphorylation site in C4-leaf phosphoenolpyruvate carboxylase from maize and sorghum."
      Jiao J.-A., Vidal J., Echevarria C., Chollet R.
      Plant Physiol. 96:297-301(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-15.
    8. "Crystal structures of C4 form maize and quaternary complex of E. coli phosphoenolpyruvate carboxylases."
      Matsumura H., Xie Y., Shirakata S., Inoue T., Yoshinaga T., Ueno Y., Izui K., Kai Y.
      Structure 10:1721-1730(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).

    Entry informationi

    Entry nameiCAPP1_MAIZE
    AccessioniPrimary (citable) accession number: P04711
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Allosteric enzyme, Direct protein sequencing

    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