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Entry version 120 (07 Apr 2021)
Sequence version 2 (23 Jan 2007)
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Protein

Diacylglycerol kinase

Gene

dgkA

Organism
Escherichia coli (strain K12)
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

Catalyzes the ATP-dependent phosphorylation of sn-l,2-diacylglycerol (DAG) to phosphatidic acid (PubMed:218816, PubMed:6277376, PubMed:6303781, PubMed:2984194, PubMed:3009449, PubMed:2828054, PubMed:9305868). Involved in the recycling of diacylglycerol produced as a by-product during membrane-derived oligosaccharide (MDO) biosynthesis (PubMed:217867, PubMed:6305970). In vitro, phosphorylates various substrates, including sn-1,2-dioleoylglycerol, sn-1,2-dioctanoylglycerol, sn-1,2-dipalmitoylglycerol, sn-1,2-dipalmitate and ceramide (PubMed:218816, PubMed:2984194, PubMed:3009449, PubMed:3021764, PubMed:2828054). Catalyzes direct phosphoryl transfer from Mg-ATP to diacylglycerol and does not form an enzyme-phosphate intermediate (PubMed:9305868).10 Publications

Miscellaneous

This small kinase has long served as a model for investigating membrane protein enzymology, folding, assembly and stability.Curated

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

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

Mg2+1 PublicationNote: Mn2+, Zn2+, Cd2+ and Co2+ support activity to lesser extents.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Requires a lipid activator for activity. Activation is observed with cardiolipin and a large number of phospholipids, sulfolipids, neutral lipids, fatty acids, alkylglycosides or detergents (PubMed:6277376, PubMed:6303781, PubMed:2984194, PubMed:3009449, PubMed:3021764, PubMed:2828054). A lipid cofactor-induced conformational change may occur as part of the activation process (PubMed:3021764). Requires a second divalent cation in addition to Mg2+-ATP (PubMed:3009449). Inhibited by the tetraphosphate-linked ATP-DAG bisubstrate analog (PubMed:9305868).7 Publications

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

  1. KM=62 µM for sn-1,2-dipalmitate1 Publication
  2. KM=230 µM for ceramide1 Publication
  3. KM=1400 µM for ATP1 Publication
  4. KM=300 µM for ATP1 Publication
  5. KM=120 µM for ATP1 Publication
  1. Vmax=10.4 µmol/min/mg enzyme1 Publication
  2. Vmax=48 µmol/min/mg enzyme with DAG as substrate1 Publication

pH dependencei

Optimum pH is 6.3-8.3.1 Publication

Temperature dependencei

Apoprotein in organic solution has an unusual stability towards heating to 100 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei10ATP2 Publications1
Binding sitei10Substrate3 Publications1
Binding sitei17ATP2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi29Divalent metal cation6 Publications1
Binding sitei29ATP2 Publications1
Binding sitei56Substrate7 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei70Proton acceptor1 Publication1
Binding sitei70Substrate5 Publications1
Metal bindingi77Divalent metal cation6 Publications1
Binding sitei77ATP2 Publications1
Binding sitei99Substrate5 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi86 – 88ATP2 Publications3
Nucleotide bindingi95 – 96ATP2 Publications2

<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

  • phosphatidic acid biosynthetic process Source: EcoCyc
  • response to UV Source: EcoCyc

<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 processLipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:DIACYLGLYKIN-MONOMER
MetaCyc:DIACYLGLYKIN-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.1.107, 2026

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000001806

<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%5Fand%5Ftaxonomy%5Fsection">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:
Diacylglycerol kinase1 Publication (EC:2.7.1.1076 Publications)
Short name:
DAGK1 Publication
Alternative name(s):
Diglyceride kinase1 Publication
Short name:
DGKCurated
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:dgkA1 Publication
Synonyms:dgk1 Publication
Ordered Locus Names:b4042, JW4002
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini2 – 31Cytoplasmic1 PublicationAdd BLAST30
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei32 – 48Helical2 PublicationsAdd BLAST17
Topological domaini49 – 51Periplasmic2 Publications3
Transmembranei52 – 69Helical2 PublicationsAdd BLAST18
Topological domaini70 – 95Cytoplasmic1 PublicationAdd BLAST26
Transmembranei96 – 119Helical1 PublicationAdd BLAST24
Topological domaini120 – 122Periplasmic2 Publications3

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mutant lacking this gene accumulates substantial amounts of diglyceride in the cytoplasmic membrane (PubMed:206553, PubMed:217867). Mutant also accumulates monoglyceride and triglyceride. Monoglyceride accumulates predominantly in the outer membrane, while triglyceride builds up together with diglyceride in the cytoplasmic membrane (PubMed:6305970).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi15A → Q: 49% of wild-type specific activity. Inactivates wild-type subunits; when associated with S-73. 1 Publication1
Mutagenesisi19W → L: 60% of wild-type activity. 41% of wild-type activity; when associated with L-26. 1 Publication1
Mutagenesisi26W → L: 23% of wild-type activity. 41% of wild-type activity; when associated with L-19. 1 Publication1
Mutagenesisi31A → L: 93% decrease in activity. 1 Publication1
Mutagenesisi70E → A, D or Q: Loss of activity. 1 Publication1
Mutagenesisi70E → C: 50% of wild-type specific activity. 1 Publication1
Mutagenesisi73N → A, Q or D: Loss of activity. 1 Publication1
Mutagenesisi73N → S: 51% of wild-type specific activity. Inactivates wild-type subunits; when associated with Q-15. 1 Publication1
Mutagenesisi77E → L: 51% of wild-type specific activity. 1 Publication1
Mutagenesisi84G → P: Loss of activity. 1 Publication1
Mutagenesisi95K → L: 54% of wild-type specific activity. 1 Publication1
Mutagenesisi96D → A: Loss of activity. 1 Publication1
Mutagenesisi96D → E: 76% decrease in activity. 1 Publication1
Mutagenesisi96D → N: 27% of wild-type specific activity. Inactivates wild-type subunits. Almost no change in activity. 2 Publications1

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001952602 – 122Diacylglycerol kinaseAdd BLAST121

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0ABN1

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

More...
PaxDbi
P0ABN1

PRoteomics IDEntifications database

More...
PRIDEi
P0ABN1

<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 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

Expression is activated by the two-component system BasRS. Repressed by sigma-E factor.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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homotrimer.

5 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4261719, 281 interactors
852837, 2 interactors

Database of interacting proteins

More...
DIPi
DIP-60228N

STRING: functional protein association networks

More...
STRINGi
511145.b4042

<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

1122
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
P0ABN1

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

More...
SMRi
P0ABN1

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0ABN1

<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>Regioni14 – 19Substrate binding4 Publications6
Regioni23 – 26Substrate binding5 Publications4
Regioni31 – 35Substrate binding6 Publications5
Regioni48 – 51Substrate binding6 Publications4
Regioni113 – 118Substrate binding7 Publications6

<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

Contains three transmembrane helices and a N-terminal amphiphilic helix located on the cytoplasmic surface (PubMed:23676677, PubMed:26673816). Residues from different subunits participate in forming the active site (PubMed:10220339, PubMed:23676677). Contains three catalytic and substrate-binding sites centred about the membrane/cytosol interface (PubMed:26673816). The gamma-phosphate of the ATP is positioned for direct transfer to the primary hydroxyl of the lipid whose acyl chain is in the membrane (PubMed:26673816).3 Publications
The presence of Trp residues has a clear effect on thermal stability. Of the mutants containing a single Trp residue, only that containing Trp-113 was found to give active protein.1 Publication

<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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG0818, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_112343_3_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0ABN1

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0ABN1

Family and domain databases

Conserved Domains Database

More...
CDDi
cd14264, DAGK_IM, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.3830.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000829, DAGK
IPR033718, DAGK_prok
IPR036945, DAGK_sf

The PANTHER Classification System

More...
PANTHERi
PTHR34299, PTHR34299, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01219, DAGK_prokar, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01069, DAGK_PROKAR, 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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P0ABN1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MANNTTGFTR IIKAAGYSWK GLRAAWINEA AFRQEGVAVL LAVVIACWLD
60 70 80 90 100
VDAITRVLLI SSVMLVMIVE ILNSAIEAVV DRIGSEYHEL SGRAKDMGSA
110 120
AVLIAIIVAV ITWCILLWSH FG
Length:122
Mass (Da):13,245
Last modified:January 23, 2007 - 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:iD5B4F86925FA6A17
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
K00127 Genomic DNA Translation: AAA24394.1
U00006 Genomic DNA Translation: AAC43136.1
U00096 Genomic DNA Translation: AAC77012.1
AP009048 Genomic DNA Translation: BAE78044.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A00667, KIECDG

NCBI Reference Sequences

More...
RefSeqi
NP_418466.1, NC_000913.3
WP_000002907.1, NZ_STEB01000022.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC77012; AAC77012; b4042
BAE78044; BAE78044; BAE78044

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
58462962
948543

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW4002
eco:b4042

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2666

<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
K00127 Genomic DNA Translation: AAA24394.1
U00006 Genomic DNA Translation: AAC43136.1
U00096 Genomic DNA Translation: AAC77012.1
AP009048 Genomic DNA Translation: BAE78044.1
PIRiA00667, KIECDG
RefSeqiNP_418466.1, NC_000913.3
WP_000002907.1, NZ_STEB01000022.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KDCNMR-A/B/C2-122[»]
3ZE3X-ray2.05A/B/C/D/E/F2-122[»]
3ZE4X-ray3.70A/B/C2-122[»]
3ZE5X-ray3.10A/B/C2-122[»]
4BPDX-ray3.30A/B/C/D/E/F2-122[»]
4BRBX-ray2.55A/B/C/D/E/F2-122[»]
4BRRX-ray2.44A/B/C/D/E/F2-122[»]
4CJZX-ray3.25A/B/C2-122[»]
4CK0X-ray2.92A/B/C2-122[»]
4D2EX-ray2.28A/B/C/D/E/F2-122[»]
4UP6X-ray3.80A/B/C2-122[»]
4UXWX-ray3.15A/B/C2-122[»]
4UXXX-ray2.70A/B/C2-122[»]
4UXZX-ray2.18A/B/C/D/E/F2-122[»]
4UYOX-ray2.18A/B/C/D/E/F2-122[»]
5D56X-ray2.80A/B/C/D/E/F2-122[»]
5D57X-ray2.80A/B/C/D/E/F2-122[»]
5D6IX-ray3.09A/B/C2-122[»]
5DWKX-ray2.60A/B/C/D/E/F2-122[»]
BMRBiP0ABN1
SMRiP0ABN1
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261719, 281 interactors
852837, 2 interactors
DIPiDIP-60228N
STRINGi511145.b4042

Chemistry databases

SwissLipidsiSLP:000001806

Proteomic databases

jPOSTiP0ABN1
PaxDbiP0ABN1
PRIDEiP0ABN1

Genome annotation databases

EnsemblBacteriaiAAC77012; AAC77012; b4042
BAE78044; BAE78044; BAE78044
GeneIDi58462962
948543
KEGGiecj:JW4002
eco:b4042
PATRICifig|1411691.4.peg.2666

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB0220

Phylogenomic databases

eggNOGiCOG0818, Bacteria
HOGENOMiCLU_112343_3_1_6
InParanoidiP0ABN1
PhylomeDBiP0ABN1

Enzyme and pathway databases

BioCyciEcoCyc:DIACYLGLYKIN-MONOMER
MetaCyc:DIACYLGLYKIN-MONOMER
BRENDAi2.7.1.107, 2026

Miscellaneous databases

EvolutionaryTraceiP0ABN1

Protein Ontology

More...
PROi
PR:P0ABN1

Family and domain databases

CDDicd14264, DAGK_IM, 1 hit
Gene3Di1.10.3830.10, 1 hit
InterProiView protein in InterPro
IPR000829, DAGK
IPR033718, DAGK_prok
IPR036945, DAGK_sf
PANTHERiPTHR34299, PTHR34299, 1 hit
PfamiView protein in Pfam
PF01219, DAGK_prokar, 1 hit
PROSITEiView protein in PROSITE
PS01069, DAGK_PROKAR, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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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 nameiKDGL_ECOLI
<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: P0ABN1
Secondary accession number(s): P00556, Q2M6R2
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 7, 2021
This is version 120 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 programProkaryotic 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, Direct protein sequencing, Reference proteome

Documents

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