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Entry version 117 (11 Dec 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Pyruvate, phosphate dikinase, chloroplastic

Gene
N/A
Organism
Flaveria bidentis (Coastal plain yellowtops) (Ethulia bidentis)
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.

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 (By similarity).By similarity
A short cytoplasmic isoform may be produced by alternative promoter usage.By similarity

<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+By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 (By similarity). Inactivated by cold due to the dissociation of the homotetramer.By similarity1 Publication

<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=73 µM for pyruvate1 Publication
  2. KM=25 µM for ATP1 Publication
  3. KM=118 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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei535Tele-phosphohistidine intermediateBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei641SubstrateBy similarity1
    Binding sitei698SubstrateBy similarity1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi827MagnesiumBy similarity1
    Binding sitei827SubstrateBy similarity1
    Binding sitei848Substrate; via carbonyl oxygenBy similarity1
    Binding sitei849Substrate; via amide nitrogenBy similarity1
    Binding sitei850SubstrateBy similarity1
    Metal bindingi851MagnesiumBy similarity1
    Binding sitei851Substrate; via amide nitrogenBy similarity1
    Active sitei913Proton donorBy similarity1

    <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 2264

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q39735

    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, chloroplastic (EC:2.7.9.1)
    Alternative name(s):
    Cold-sensitive pyruvate, orthophosphate dikinase
    Pyruvate, orthophosphate dikinase
    <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>OrganismiFlaveria bidentis (Coastal plain yellowtops) (Ethulia bidentis)
    <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 identifieri4224 [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 lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaeasteridscampanulidsAsteralesAsteraceaeAsteroideaeHeliantheae allianceTageteaeFlaveria

    <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 & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Chloroplast, 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>Mutagenesisi869Q → P: 60% activity in the cold. 60% activity in the cold; when associated with S-873. 1 Publication1
    Mutagenesisi873A → S: 10% activity in the cold. 60% activity in the cold; when associated with P-869. 1 Publication1
    Mutagenesisi885I → L: 50% activity in the cold. 65% activity in the cold; when associated with V-952. 1 Publication1
    Mutagenesisi952I → V: 25% activity in the cold. 65% activity in the cold; when associated with L-885. 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 – 77Chloroplast1 PublicationAdd BLAST77
    <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_000002355978 – 953Pyruvate, phosphate dikinase, chloroplasticAdd BLAST876

    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 residuei533Phosphothreonine; by PDRP1By similarity1

    <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-533 in the dark inactivates the enzyme. Dephosphorylation upon light stimulation reactivates the enzyme (By similarity).By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q39735

    <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.

    <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

    3D structure databases

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

    More...
    SMRi
    Q39735

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    <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.By similarity
    The C-terminal domain (829-953) is involved in cold sensitivity.

    <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

    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 PTHR22931, 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, 2 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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

    <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.

    Q39735-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MMSSLSVEGM LLKSARESCL PARVNQRRNG DLRRLNHHRQ SSFVRCLTPA
    60 70 80 90 100
    RVSRPELRSS GLTPPRAVLN PVSPPVTTAK KRVFTFGKGR SEGNRDMKSL
    110 120 130 140 150
    LGGKGANLAE MSSIGLSVPP GLTISTEACE EYQQNGKSLP PGLWDEISEG
    160 170 180 190 200
    LDYVQKEMSA SLGDPSKPLP LSVRSGAAIS MPGMMDTVLN LGLNDEVVAG
    210 220 230 240 250
    LAGKSGARFA YDSYRRFLDM FGNVVMGIPH SLFDEKLEQM KAEKGIHLDT
    260 270 280 290 300
    DLTAADLKDL VEKYKNVYVE AKGEKFPTDP KKQLELAVNA VFDSWDSPRA
    310 320 330 340 350
    NKYRSINQIT GLKGTAVNIQ SMVFGNMGNT SGTGVLFTRN PSTGEKKLYG
    360 370 380 390 400
    EFLINAQGED VVAGIRTPED LGTMETCMPD AYKELVENCE ILEGHYKDMM
    410 420 430 440 450
    DIEFTVQENR LWMLQCRTGK RTGKGAVRIA VDMVNEWLID TRTAIKRVET
    460 470 480 490 500
    QHLDQLLHPQ FEDPSAYKSH VVATGLPASP GAAVGQVCFS AEDAETWHAQ
    510 520 530 540 550
    GKSAILVRTE TSPEDVGGMH AAAGILTARG GMTSHAAVVA RGWGKCCVSG
    560 570 580 590 600
    CADIRVNDDM KIFTIGDRVI KEGDWLSLNG TTGEVILGKQ LLAPPAMSND
    610 620 630 640 650
    LEIFMSWADQ ARRLKVMANA DTPNDALTAR NNGAQGIGLC RTEHMFFASD
    660 670 680 690 700
    ERIKAVRKMI MAVTPEQRKV ALDLLLPYQR SDFEGIFRAM DGLPVTIRLL
    710 720 730 740 750
    DPPLHEFLPE GDLEHIVNEL AVDTGMSADE IYSKIENLSE VNPMLGFRGC
    760 770 780 790 800
    RLGISYPELT EMQVRAIFQA AVSMTNQGVT VIPEIMVPLV GTPQELRHQI
    810 820 830 840 850
    SVIRGVAANV FAEMGVTLEY KVGTMIEIPR AALIAEEIGK EADFFSFGTN
    860 870 880 890 900
    DLTQMTFGYS RDDVGKFLQI YLAQGILQHD PFEVIDQKGV GQLIKMATEK
    910 920 930 940 950
    GRAANPNLKV GICGEHGGEP SSVAFFDGVG LDYVSCSPFR VPIARLAAAQ

    VIV
    Length:953
    Mass (Da):104,002
    Last modified:November 1, 1996 - v1
    <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:i7BEC5276C1C1DC4C
    GO

    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
    U08400 mRNA Translation: AAA86941.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S56650

    <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
    U08400 mRNA Translation: AAA86941.1
    PIRiS56650

    3D structure databases

    SMRiQ39735
    ModBaseiSearch...

    Proteomic databases

    PRIDEiQ39735

    Enzyme and pathway databases

    UniPathwayiUPA00322
    BRENDAi2.7.9.1 2264
    SABIO-RKiQ39735

    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 PTHR22931, 1 hit
    PfamiView protein in Pfam
    PF00391 PEP-utilizers, 1 hit
    PF02896 PEP-utilizers_C, 1 hit
    PF01326 PPDK_N, 2 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...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    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 nameiPPDK_FLABI
    <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: Q39735
    <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 15, 1998
    Last sequence update: November 1, 1996
    Last modified: December 11, 2019
    This is version 117 of the entry and version 1 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

    Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
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