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Entry version 104 (11 Dec 2019)
Sequence version 1 (01 Oct 1996)
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Protein

Pyruvate, phosphate dikinase

Gene
N/A
Organism
Giardia intestinalis (Giardia lamblia)
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.

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 <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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei99ATPSequence analysis1
<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 sitei464Tele-phosphohistidine intermediateBy similarity1
Binding sitei570SubstrateBy similarity1
Binding sitei626SubstrateBy 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 bindingi753MagnesiumBy similarity1
Binding sitei753SubstrateBy similarity1
Binding sitei774Substrate; via carbonyl oxygenBy similarity1
Binding sitei775Substrate; via amide nitrogenBy similarity1
Binding sitei776SubstrateBy similarity1
Metal bindingi777MagnesiumBy similarity1
Binding sitei777Substrate; 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

<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 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>OrganismiGiardia intestinalis (Giardia lamblia)
<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 identifieri5741 [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 lineageiEukaryotaMetamonadaDiplomonadidaHexamitidaeGiardiinaeGiardia

<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_00001470521 – 884Pyruvate, phosphate dikinaseAdd BLAST884

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 residuei462Phosphothreonine; 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-462 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
P51776

<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

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
5741.EDO77898

<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

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SMRi
P51776

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

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 – 351N-terminalAdd BLAST351
Regioni352 – 408Linker 1Add BLAST57
Regioni409 – 507CentralAdd BLAST99
Regioni508 – 542Linker 2Add BLAST35
Regioni543 – 884C-terminalAdd BLAST342

<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

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
3.20.20.60, 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.

P51776-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSTRRVYFFG ETPENQPANS ELCRKVLGGK GISLAAMIKL GMPVPLGFTI
60 70 80 90 100
TCQTCVEYQK TASWPKGLKE EVASNLKLLE EKMGKTFGDN TNPLLVSVRS
110 120 130 140 150
GAAVSMPGMM DTILNLGLND ESVKGLAAVT GNARFAYDSY RRFMQMFGDV
160 170 180 190 200
CLGIDHDKFE HALDAVKTRY GRKTDPELTA DELEEVCEAY RKICVAATGK
210 220 230 240 250
TFPQCPHEQL ELAINAVFKS WTNPRAQAYR TLNKLDHNMG TAVNVQSMVF
260 270 280 290 300
GNTGDDSGTG VGFTRCPKTG EKFSYLYGEF LQNAQGEDVV AGIRTPVNLK
310 320 330 340 350
EMPTINASWK ACYDELSLIY AKLEGYYNDM VDLEFTVENG KLWMLQARAG
360 370 380 390 400
KRTGFAMVRI AIDMCKEGML TEEEALLRID ANKINEFLFK RFDPSVKPVV
410 420 430 440 450
LGKGIPASPG AAVGVICFCP MRTCELAEQG KKVILTRIET SPEDILGMDR
460 470 480 490 500
AVGILTARGG QTSHAAVVAR GMGKCCVAGA DCCQINYATK TLVIGDRKFK
510 520 530 540 550
EGDFISINGT TGEIYNGAVQ TIEPGITDDL QTIMDWSDKY RVLKIRTNAD
560 570 580 590 600
TPHDAAVARK FGAEGIGLCR TEHMFFAADR IMAMREMILS DDEGARRTAL
610 620 630 640 650
NKLLPFQRED FIGIFKAMDG KGVNIRLLDP PLHEFLPHTR DLQKKLAEDM
660 670 680 690 700
NKKHRHIHER VEDLHEVNPM LGFRGVRLGI VYPEISEMQV RAILEAACIV
710 720 730 740 750
SREGVTVKPE IMIPVLFSEN EMEIMHALVN RVAASVFKEH GTTVDYEVGT
760 770 780 790 800
MIELPRACVM ADKIAQTAQY FSFGTNDLTQ TTFGISRDDA GKFIPKYIDR
810 820 830 840 850
GIFKVDPFVT LDQQGVGALM KMAIEGGRST RTDMKIGICG EQTDPASILF
860 870 880
LHKIGLNYVS CSPYRVPVAR VAAAIAAIKA RTNQ
Length:884
Mass (Da):97,630
Last modified:October 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:i82E2BE9C09C0E772
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
Z54168 Genomic DNA Translation: CAA90880.1

<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
Z54168 Genomic DNA Translation: CAA90880.1

3D structure databases

SMRiP51776
ModBaseiSearch...

Protein-protein interaction databases

STRINGi5741.EDO77898

Proteomic databases

PRIDEiP51776

Phylogenomic databases

eggNOGiENOG410IIM3 Eukaryota
COG0574 LUCA

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_GIAIN
<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: P51776
<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, 1996
Last sequence update: October 1, 1996
Last modified: December 11, 2019
This is version 104 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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