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Protein

Pyruvate, phosphate dikinase 1, chloroplastic

Gene

PPDK1

Organism
Zea mays (Maize)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Formation of phosphoenolpyruvate, which is the primary acceptor of CO2 in C4 and some Crassulacean acid metabolism plants.2 Publications

Miscellaneous

The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain.
PubMed:1668653 shows the existence of a second gene coding only for the short cytoplasmic isoform of PPDK.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+1 Publication1 Publication

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Activated by light-induced dephosphorylation. Inhibited by dark-induced phosphorylation. Both reactions are catalyzed by PDRP1. Inactivated by cold due to the dissociation of the homotetramer. Independent of circadian regulation (PubMed:24710069).4 Publications

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=158 µM for pyruvate1 Publication
  2. KM=178 µM for pyruvate1 Publication
  3. KM=95 µM for ATP1 Publication
  4. KM=194 µM for phosphoenolpyruvate1 Publication
  5. KM=408 µM for phosphate1 Publication

    Temperature dependencei

    Loss of activity below 10 degrees Celsius.1 Publication

    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>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
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei529Tele-phosphohistidine intermediate1 Publication1
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei635Substrate1 Publication1
    Binding sitei692Substrate1 Publication1
    <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi821Magnesium1 Publication1
    Binding sitei821Substrate1 Publication1
    Binding sitei842Substrate; via carbonyl oxygen1 Publication1
    Binding sitei843Substrate; via amide nitrogen1 Publication1
    Binding sitei844Substrate1 Publication1
    Metal bindingi845Magnesium1 Publication1
    Binding sitei845Substrate; via amide nitrogen1 Publication1
    Active sitei907Proton donor1 Publication1

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionKinase, Transferase
    Biological processPhotosynthesis
    LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.7.9.1 6752

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P11155

    UniPathway: a resource for the exploration and annotation of metabolic pathways

    More...
    UniPathwayi
    UPA00322

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
    Recommended name:
    Pyruvate, phosphate dikinase 1, chloroplastic1 Publication (EC:2.7.9.14 Publications)
    Alternative name(s):
    Pyruvate, orthophosphate dikinase 1
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:PPDK11 Publication
    Synonyms:C4PPDKZM11 Publication, CYPPDKZM11 Publication, PPDK21 Publication
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiZea mays (Maize)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri4577 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogonodaeAndropogoneaeTripsacinaeZea
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000007305 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

    Organism-specific databases

    Maize Genetics and Genomics Database

    More...
    MaizeGDBi
    25385

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Chloroplast, Cytoplasm, Plastid

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi525G → A or P: Greatly reduced activity. Strongly reduced or lack of phosphorylation by PDRP1 in vitro. 1 Publication1
    Mutagenesisi527T → D or E: Abolished activity. 2 Publications1
    Mutagenesisi527T → N: Greatly reduced activity. 2 Publications1
    Mutagenesisi527T → S or V: No effect on activity. 2 Publications1
    Mutagenesisi527T → Y: Greatly reduced activity. No tyrosine phosphorylation by PDRP1 in vitro. 2 Publications1
    Mutagenesisi528S → C: No effect on activity or phosphorylation by PDRP1 in vitro. 1 Publication1
    Mutagenesisi528S → Y or T: Greatly reduced activity. Strongly reduced or lack of phosphorylation by PDRP1 in vitro. 1 Publication1
    Mutagenesisi529H → N: Abolished activity. No phosphorylation on T-527 by PDRP1 in vitro. 1 Publication1
    Mutagenesisi946L → V: No decrease of the cold sensitivity. 1 Publication1

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 62Chloroplast1 PublicationAdd BLAST62
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000043171463 – 947Pyruvate, phosphate dikinase 1, chloroplasticAdd BLAST885

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei63N-acetylalanine; partial1 Publication1
    Modified residuei309Phosphothreonine1 Publication1
    Modified residuei506Phosphoserine1 Publication1
    Modified residuei527Phosphothreonine; by PDRP13 Publications1
    Modified residuei528Phosphoserine; by PDRP11 Publication1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

    Phosphorylation of Thr-527 in the dark inactivates the enzyme, dephosphorylation upon light stimulation reactivates the enzyme (PubMed:2834385). More highly phosphorylated when grown under high rather than low light regimes (70 vs 900 µmol photons/m-2/s). the degree of phosphorylation is strictly regulated by light intensity and the light/dark transition has no influence (PubMed:24710069). Phosphorylated in both mesophyll and bundle sheath cells (PubMed:22833285). The phosphorylation at Ser-528 may be important for the phosphorylation at Thr-527 and may also be regulated by light intensity (PubMed:24710069).3 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    P11155

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P11155

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P11155

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

    Isoform C4PPDKZM1 mainly localized in mesophyll cells and only a low level is found in bundle sheath cells. Isoform CYPPDKZM1 expressed in roots, stems and etiolated leaves.3 Publications

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Isoform C4ppdkZm1 is light-inducible.2 Publications

    Gene expression databases

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P11155 baseline and differential

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

    Homotetramer.1 Publication

    Protein-protein interaction databases

    STRING: functional protein association networks

    More...
    STRINGi
    4577.GRMZM2G306345_P05

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1947
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1VBGX-ray2.30A72-947[»]
    1VBHX-ray2.30A72-947[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    P11155

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    P11155

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...
    EvolutionaryTracei
    P11155

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

    The N-terminal domain contains the ATP/Pi binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site.

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Belongs to the PEP-utilizing enzyme family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    COG0574 LUCA

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.20.20.60, 1 hit
    3.30.1490.20, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR013815 ATP_grasp_subdomain_1
    IPR008279 PEP-util_enz_mobile_dom
    IPR018274 PEP_util_AS
    IPR000121 PEP_util_C
    IPR023151 PEP_util_CS
    IPR036637 Phosphohistidine_dom_sf
    IPR002192 PPDK_PEP-bd
    IPR010121 Pyruvate_phosphate_dikinase
    IPR015813 Pyrv/PenolPyrv_Kinase-like_dom
    IPR040442 Pyrv_Kinase-like_dom_sf

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR22931:SF9 PTHR22931:SF9, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00391 PEP-utilizers, 1 hit
    PF02896 PEP-utilizers_C, 1 hit
    PF01326 PPDK_N, 3 hits

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000853 PPDK, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51621 SSF51621, 1 hit
    SSF52009 SSF52009, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01828 pyru_phos_dikin, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00742 PEP_ENZYMES_2, 1 hit
    PS00370 PEP_ENZYMES_PHOS_SITE, 1 hit

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative promoter usage. AlignAdd to basket
    Isoform C4PPDKZM11 Publication (identifier: P11155-1) [UniParc]FASTAAdd to basket
    Also known as: C4PPDK1 Publication

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide
            10         20         30         40         50
    MAASVSRAIC VQKPGSKCTR DREATSFARR SVAAPRPPHA KAAGVIRSDS
    60 70 80 90 100
    GAGRGQHCSP LRAVVDAAPI QTTKKRVFHF GKGKSEGNKT MKELLGGKGA
    110 120 130 140 150
    NLAEMASIGL SVPPGFTVST EACQQYQDAG CALPAGLWAE IVDGLQWVEE
    160 170 180 190 200
    YMGATLGDPQ RPLLLSVRSG AAVSMPGMMD TVLNLGLNDE VAAGLAAKSG
    210 220 230 240 250
    ERFAYDSFRR FLDMFGNVVM DIPRSLFEEK LEHMKESKGL KNDTDLTASD
    260 270 280 290 300
    LKELVGQYKE VYLSAKGEPF PSDPKKQLEL AVLAVFNSWE SPRAKKYRSI
    310 320 330 340 350
    NQITGLRGTA VNVQCMVFGN MGNTSGTGVL FTRNPNTGEK KLYGEFLVNA
    360 370 380 390 400
    QGEDVVAGIR TPEDLDAMKN LMPQAYDELV ENCNILESHY KEMQDIEFTV
    410 420 430 440 450
    QENRLWMLQC RTGKRTGKSA VKIAVDMVNE GLVEPRSAIK MVEPGHLDQL
    460 470 480 490 500
    LHPQFENPSA YKDQVIATGL PASPGAAVGQ VVFTAEDAEA WHSQGKAAIL
    510 520 530 540 550
    VRAETSPEDV GGMHAAVGIL TERGGMTSHA AVVARWWGKC CVSGCSGIRV
    560 570 580 590 600
    NDAEKLVTIG SHVLREGEWL SLNGSTGEVI LGKQPLSPPA LSGDLGTFMA
    610 620 630 640 650
    WVDDVRKLKV LANADTPDDA LTARNNGAQG IGLCRTEHMF FASDERIKAV
    660 670 680 690 700
    RQMIMAPTLE LRQQALDRLL TYQRSDFEGI FRAMDGLPVT IRLLDHPSYE
    710 720 730 740 750
    FLPEGNIEDI VSELCAETGA NQEDALARIE KLSEVNPMLG FRGCRLGISY
    760 770 780 790 800
    PELTEMQARA IFEAAIAMTN QGVQVFPEIM VPLVGTPQEL GHQVTLIRQV
    810 820 830 840 850
    AEKVFANVGK TIGYKVGTMI EIPRAALVAD EIAEQAEFFS FGTNDLTQMT
    860 870 880 890 900
    FGYSRDDVGK FIPVHLAQGI LQHDPFEVLD QRGVGELVKF ATERGRKARP
    910 920 930 940
    NLKVGICGEH GGEPSSVAFF AKAGLDFVSC SPFRVPIARL AAAQVLV
    Length:947
    Mass (Da):102,674
    Last modified:July 1, 2008 - v2
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6D11F51D150ACFD1
    GO
    Isoform CYPPDKZM12 Publications (identifier: P11155-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-75: MAASVSRAIC...DAAPIQTTKK → MAPVQCARSQ

    Note: Produced by alternative promoter usage (PubMed:1668653). Cytoplasmic (PubMed:1668653). Initiator Met-1 is removed (PubMed:24710069).2 Publications
    Show »
    Length:882
    Mass (Da):95,968
    Checksum:i2836A730291B5524
    GO

    <p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

    The sequence AAA33495 differs from that shown. Reason: Frameshift at positions 43 and 56.Curated

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti2A → T in AAA33498 (PubMed:2170354).Curated1
    Sequence conflicti2A → T in AAB23730 (PubMed:1668653).Curated1
    Sequence conflicti218Missing in ACR78549 (PubMed:19329568).Curated1
    Sequence conflicti404R → G in ACR78549 (PubMed:19329568).Curated1
    Sequence conflicti536W → G in AAA33498 (PubMed:2170354).Curated1
    Sequence conflicti536W → G in ACR78549 (PubMed:19329568).Curated1
    Sequence conflicti561S → G in AAA33498 (PubMed:2170354).Curated1
    Sequence conflicti561S → G in ACR78549 (PubMed:19329568).Curated1
    Sequence conflicti671T → P in AAA33498 (PubMed:2170354).Curated1
    Sequence conflicti671T → P in ACR78549 (PubMed:19329568).Curated1
    Sequence conflicti696 – 699HPSY → PPLH in AAA33498 (PubMed:2170354).Curated4
    Sequence conflicti696 – 699HPSY → PPLH in ACR78549 (PubMed:19329568).Curated4
    Sequence conflicti760A → V in ACR78549 (PubMed:19329568).Curated1
    Sequence conflicti865H → Y in AAA33498 (PubMed:2170354).Curated1
    Sequence conflicti865H → Y in ACR78549 (PubMed:19329568).Curated1
    Sequence conflicti869 – 873GILQH → EFGTS in AAD45281 (Ref. 8) Curated5
    Sequence conflicti878V → I in ACR78549 (PubMed:19329568).Curated1
    Sequence conflicti890F → L in AAA33498 (PubMed:2170354).Curated1
    Sequence conflicti890F → L in ACR78549 (PubMed:19329568).Curated1
    Sequence conflicti927F → Y in AAA33498 (PubMed:2170354).Curated1
    Sequence conflicti927F → Y in AAD45281 (Ref. 8) Curated1
    Sequence conflicti927F → Y in ACR78549 (PubMed:19329568).Curated1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0573731 – 75MAASV…QTTKK → MAPVQCARSQ in isoform CYPPDKZM1. Add BLAST75

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    DDBJi
    Links Updated
    J03901 mRNA Translation: AAA33495.1 Frameshift.
    M58656, M58655 Genomic DNA Translation: AAA33498.1
    S46966 Genomic DNA Translation: AAB23731.1
    S46965, S46964 Genomic DNA Translation: AAB23730.1
    X14927 Genomic DNA Translation: CAA33054.1
    FJ935764 Genomic DNA Translation: ACR78549.1
    AF152599 mRNA Translation: AAD45281.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A29225 KIZMPO
    PQ0190

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Zm.19489

    Keywords - Coding sequence diversityi

    Alternative promoter usage

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J03901 mRNA Translation: AAA33495.1 Frameshift.
    M58656, M58655 Genomic DNA Translation: AAA33498.1
    S46966 Genomic DNA Translation: AAB23731.1
    S46965, S46964 Genomic DNA Translation: AAB23730.1
    X14927 Genomic DNA Translation: CAA33054.1
    FJ935764 Genomic DNA Translation: ACR78549.1
    AF152599 mRNA Translation: AAD45281.1
    PIRiA29225 KIZMPO
    PQ0190
    UniGeneiZm.19489

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1VBGX-ray2.30A72-947[»]
    1VBHX-ray2.30A72-947[»]
    ProteinModelPortaliP11155
    SMRiP11155
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi4577.GRMZM2G306345_P05

    PTM databases

    iPTMnetiP11155

    Proteomic databases

    PaxDbiP11155
    PRIDEiP11155

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Organism-specific databases

    MaizeGDBi25385

    Phylogenomic databases

    eggNOGiCOG0574 LUCA

    Enzyme and pathway databases

    UniPathwayi
    UPA00322

    BRENDAi2.7.9.1 6752
    SABIO-RKiP11155

    Miscellaneous databases

    EvolutionaryTraceiP11155

    Gene expression databases

    ExpressionAtlasiP11155 baseline and differential

    Family and domain databases

    Gene3Di3.20.20.60, 1 hit
    3.30.1490.20, 1 hit
    InterProiView protein in InterPro
    IPR013815 ATP_grasp_subdomain_1
    IPR008279 PEP-util_enz_mobile_dom
    IPR018274 PEP_util_AS
    IPR000121 PEP_util_C
    IPR023151 PEP_util_CS
    IPR036637 Phosphohistidine_dom_sf
    IPR002192 PPDK_PEP-bd
    IPR010121 Pyruvate_phosphate_dikinase
    IPR015813 Pyrv/PenolPyrv_Kinase-like_dom
    IPR040442 Pyrv_Kinase-like_dom_sf
    PANTHERiPTHR22931:SF9 PTHR22931:SF9, 1 hit
    PfamiView protein in Pfam
    PF00391 PEP-utilizers, 1 hit
    PF02896 PEP-utilizers_C, 1 hit
    PF01326 PPDK_N, 3 hits
    PIRSFiPIRSF000853 PPDK, 1 hit
    SUPFAMiSSF51621 SSF51621, 1 hit
    SSF52009 SSF52009, 1 hit
    TIGRFAMsiTIGR01828 pyru_phos_dikin, 1 hit
    PROSITEiView protein in PROSITE
    PS00742 PEP_ENZYMES_2, 1 hit
    PS00370 PEP_ENZYMES_PHOS_SITE, 1 hit

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPPDK1_MAIZE
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P11155
    Secondary accession number(s): C5IHE0
    , Q41846, Q41847, Q42367, Q7DMU6, Q9XGW9
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: July 1, 2008
    Last modified: January 16, 2019
    This is version 148 of the entry and version 2 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
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