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Entry version 124 (11 Dec 2019)
Sequence version 2 (23 Nov 2004)
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Protein

Pyruvate, phosphate dikinase, chloroplastic

Gene

PPDK

Organism
Flaveria trinervia (Clustered yellowtops) (Oedera trinervia)
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

<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).By similarity

<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, Pyruvate

Enzyme and pathway databases

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:2.7.9.1By similarity)
Alternative name(s):
Pyruvate, orthophosphate dikinase
<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:PPDK
Synonyms:PDK
<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 trinervia (Clustered yellowtops) (Oedera trinervia)
<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 identifieri4227 [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, Cytoplasm, Plastid

<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 – 77ChloroplastBy similarityAdd 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_000002356278 – 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
P22221

<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 1 mainly localized in mesophyll cells and only a low level is found in bundle sheath cells. Isoform 2 is expressed in roots and stems.1 Publication

<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 1 is light-inducible while isoform 2 is dark-inducible.1 Publication

<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.

By similarity

<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

1953
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P22221

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

<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>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 1 (identifier: P22221-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
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 SLGDPSKPLL 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 LGTMETCMPE AYKELVENCE ILERHYKDMM
410 420 430 440 450
DIEFTVQENR LWMLQCRTGK RTGKGAVRIA VDMVNEGLID 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
GRAANPSLKV GICGEHGGEP SSVAFFDGVG LDYVSCSPFR VPIARLAAAQ

VIV
Length:953
Mass (Da):103,975
Last modified:November 23, 2004 - 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:i9C13CA6C06A8F7C6
GO
Isoform 2 (identifier: P22221-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-79: Missing.
     80-81: KK → MQ

Note: Produced by alternative promoter usage. Cytoplasmic.Curated
Show »
Length:874
Mass (Da):95,248
Checksum:i12DFF5FF9965CE9A
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 CAA55702 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAA55703 differs from that shown. Reason: Erroneous gene model prediction.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 conflicti143L → S in CAA40420 (PubMed:2172023).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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0346071 – 79Missing in isoform 2. CuratedAdd BLAST79
Alternative sequenceiVSP_03460880 – 81KK → MQ in isoform 2. Curated2

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
X57141 mRNA Translation: CAA40420.1
X79095 Genomic DNA Translation: CAA55702.1 Sequence problems.
X79095 Genomic DNA Translation: CAA55703.1 Sequence problems.

Protein sequence database of the Protein Information Resource

More...
PIRi
S12894
S61410

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
X57141 mRNA Translation: CAA40420.1
X79095 Genomic DNA Translation: CAA55702.1 Sequence problems.
X79095 Genomic DNA Translation: CAA55703.1 Sequence problems.
PIRiS12894
S61410

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
5JVJX-ray2.90A/B80-953[»]
5JVLX-ray2.90A/B/C/D80-953[»]
5LU4X-ray2.90A/B80-953[»]
SMRiP22221
ModBaseiSearch...
PDBe-KBiSearch...

Proteomic databases

PRIDEiP22221

Enzyme and pathway databases

UniPathwayiUPA00322

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_FLATR
<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: P22221
Secondary accession number(s): Q42738, Q42739
<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: August 1, 1991
Last sequence update: November 23, 2004
Last modified: December 11, 2019
This is version 124 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

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
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