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Protein

Pyruvate, phosphate dikinase

Gene

PPDK

Organism
Entamoeba histolytica
Status
Reviewed-Annotation score:

Annotation score:4 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>
-Protein inferred from homologyi <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

Catalyzes the reversible phosphorylation of pyruvate and phosphate. In E.histolytica and C.symbiosus, PPDK functions in the direction of ATP synthesis.

Miscellaneous

The reaction takes place in three steps, each mediated by a carrier 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.

<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 ‘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 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei91ATPSequence analysis1
<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 sitei454Tele-phosphohistidine intermediateBy similarity1
Binding sitei561SubstrateBy similarity1
Binding sitei617SubstrateBy similarity1
<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 bindingi752MagnesiumBy similarity1
Binding sitei752SubstrateBy similarity1
Binding sitei773Substrate; via carbonyl oxygenBy similarity1
Binding sitei774Substrate; via amide nitrogenBy similarity1
Binding sitei775SubstrateBy similarity1
Metal bindingi776MagnesiumBy similarity1
Binding sitei776Substrate; via amide nitrogenBy similarity1
Active sitei839Proton 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
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.9.1 2080

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P37213

<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 (EC:2.7.9.1)
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
<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>OrganismiEntamoeba histolytica
<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 identifieri5759 [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 lineageiEukaryotaAmoebozoaArchamoebaeEntamoebidaeEntamoeba

<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 polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001470511 – 885Pyruvate, phosphate dikinaseAdd 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 residuei452Phosphothreonine; 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-452 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
P37213

<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

Homodimer.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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P37213

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

More...
SMRi
P37213

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 342N-terminalAdd BLAST342
Regioni343 – 399Linker 1Add BLAST57
Regioni400 – 497CentralAdd BLAST98
Regioni498 – 533Linker 2Add BLAST36
Regioni534 – 885C-terminalAdd BLAST352

<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 active site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate active 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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IIM3 Eukaryota
COG0574 LUCA

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
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

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>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.

P37213-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQRVYAFEDG DGTNKKLLGG KGAGLCTMTK IGLPVPQGFV ITTEMCKQFI
60 70 80 90 100
ANGNKMPEGL MEEVKKEYQL VEKKSGKVFG GEENPLLVSV RSGAAMSMPG
110 120 130 140 150
MMDTILNLGL NDKTVVALAK LTNNERFAYD SYRRFVSLFG KIALNACDEV
160 170 180 190 200
YDKTLENKKV EKGVKLDTEL DANDMKELAQ VFIKKTEEFT KQPFPVDPYA
210 220 230 240 250
QLEFAICAVF RSWMGKRAVD YRREFKITPE QADGTAVSVV SMVYGNMGND
260 270 280 290 300
SATGVCFTRD PGTGENMFFG EYLKNAQGED VVAGIRTPQI ISKMAEDRDL
310 320 330 340 350
PGCYEQLLDI RKKLEGYFHE VQDFEFTIER KKLYMLQTRN GKMNATATVR
360 370 380 390 400
TGVDMVEEGL ITKEQAIMRI APQSVDQLLH KNMPANYAEA PLVKGLPASP
410 420 430 440 450
GAATGAVVFD ADDAVEQAKG KKVLLLREET KPEDIHGFFV AEGILTCRGG
460 470 480 490 500
KTSHAAVVAR GMGKPCVSGA EGIKVDVAKK IAKIGSLEVH EGDILTIDGS
510 520 530 540 550
TGCVYKGEVP LEEPQVGSGY FGTILKWANE IKKIGVFAAG DLPSAAKKAL
560 570 580 590 600
EFGAEGIGLC RTERMFNAVE RLPIVVKMIL SNTLEERKKY LNELMPLQKQ
610 620 630 640 650
DFIGLLKTMN GLPVTVRLLD PPLHEFLPTL EELMREIFEM KLSGKTEGLA
660 670 680 690 700
EKEVVLKKVK ELMEVNPMIG HRGIRLGTTN PEIYEMQIRA FLEATREVIK
710 720 730 740 750
EGINDHREIM IPNVTEVNEL INLRKNVLEP VHEEVEKKYG IKVPFSYGTM
760 770 780 790 800
VECVRAALTA DKIATEASFF SFGTNDLTQG TFSYSREDSE NKFIPKYVEL
810 820 830 840 850
KILPANPFEI LDRPGVGEVM RIAVTKGRQT RPELLVGICG EHGGEPSSIE
860 870 880
WCHMIGLNYV SCSSYRIPVA RIAAAQAQIR HPREN
Length:885
Mass (Da):98,060
Last modified:October 1, 1994 - 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:i6F5FEAD7C21CC8DC
GO

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 conflicti539 – 540AG → NA in AAA19026 (PubMed:1340319).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
X74596 Genomic DNA Translation: CAA52673.1
L03389 Unassigned DNA Translation: AAA19026.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S36601

<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
X74596 Genomic DNA Translation: CAA52673.1
L03389 Unassigned DNA Translation: AAA19026.1
PIRiS36601

3D structure databases

ProteinModelPortaliP37213
SMRiP37213
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiP37213

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IIM3 Eukaryota
COG0574 LUCA

Enzyme and pathway databases

BRENDAi2.7.9.1 2080
SABIO-RKiP37213

Family and domain databases

Gene3Di3.30.1490.20, 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
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 nameiPPDK_ENTHI
<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: P37213
<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: October 1, 1994
Last sequence update: October 1, 1994
Last modified: December 5, 2018
This is version 109 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)

<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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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