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Entry version 112 (08 May 2019)
Sequence version 2 (23 Jan 2007)
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Protein

D-erythrose-4-phosphate dehydrogenase

Gene

epd

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 NAD-dependent conversion of D-erythrose 4-phosphate to 4-phosphoerythronate.2 Publications

Caution

Was originally (PubMed:2546007 and PubMed:2124629) thought to be a glyceraldehyde 3-phosphate dehydrogenase, but glyceraldehyde 3-phosphate is not an efficient substrate (PubMed:7751290 and PubMed:9182530).Curated

<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 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=74 µM for NAD (at 37 degrees Celsius and pH 8.6)2 Publications
  2. KM=510 µM for D-erythrose 4-phosphate (at 25 degrees Celsius and pH 8.9)2 Publications
  3. KM=960 µM for D-erythrose 4-phosphate (at 37 degrees Celsius and pH 8.6)2 Publications
  4. KM=1100 µM for glyceraldehyde 3-phosphate (at 25 degrees Celsius and pH 8.9)2 Publications
  1. Vmax=91.2 µmol/min/mg enzyme toward D-erythrose 4-phosphate (at 37 degrees Celsius and pH 8.6)2 Publications
  2. Vmax=77.2 µmol/min/mg enzyme toward NAD (at 37 degrees Celsius and pH 8.6)2 Publications

pH dependencei

Optimum pH is about 8.6.2 Publications

Temperature dependencei

Optimum temperature is 50 degrees Celsius at pH 8.6. Relatively thermostable. Activity begins to decrease significantly when E4PDH is incubated at 50 degrees Celsius for 5 min.2 Publications

<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: pyridoxine 5'-phosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes pyridoxine 5'-phosphate from D-erythrose 4-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. D-erythrose-4-phosphate dehydrogenase (epd)
  2. Erythronate-4-phosphate dehydrogenase (pdxB)
  3. Phosphoserine aminotransferase (serC)
  4. 4-hydroxythreonine-4-phosphate dehydrogenase (pdxA)
  5. Pyridoxine 5'-phosphate synthase (pdxJ)
This subpathway is part of the pathway pyridoxine 5'-phosphate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyridoxine 5'-phosphate from D-erythrose 4-phosphate, the pathway pyridoxine 5'-phosphate biosynthesis and in Cofactor biosynthesis.

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 sitei81NAD; via carbonyl oxygenBy similarity1
<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 sitei155NucleophileBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei182Activates thiol group during catalysisBy similarity1
Binding sitei200SubstrateSequence analysis1
Binding sitei236SubstrateSequence analysis1
Binding sitei318NADBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 bindingi12 – 13NADBy similarity2

<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 functionOxidoreductase
Biological processPyridoxine biosynthesis
LigandNAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:ERYTH4PDEHYDROG-MONOMER
ECOL316407:JW2894-MONOMER
MetaCyc:ERYTH4PDEHYDROG-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.2.1.72 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P0A9B6

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00244;UER00309

<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:
D-erythrose-4-phosphate dehydrogenase (EC:1.2.1.72)
Short name:
E4PDH
<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:epd
Synonyms:gapB
Ordered Locus Names:b2927, JW2894
<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>OrganismiEscherichia coli (strain K12)
<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 identifieri83333 [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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_manual">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

Organism-specific databases

Escherichia coli strain K12 genome database

More...
EcoGenei
EG10368 epd

<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

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi155C → A, G or V: No significant activity. 1 Publication1
Mutagenesisi182H → N: 10-fold reduction in activity. Increases affinity for D-erythrose-4-phosphate and reduces affinity for glyceraldehyde 3-phosphate. 1 Publication1
Mutagenesisi316C → A or Y: Reduces activity and affinity for D-erythrose-4-phosphate and increases affinity for glyceraldehyde 3-phosphate. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001456502 – 339D-erythrose-4-phosphate dehydrogenaseAdd BLAST338

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A9B6

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

More...
PaxDbi
P0A9B6

PRoteomics IDEntifications database

More...
PRIDEi
P0A9B6

<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.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4262067, 12 interactors

Database of interacting proteins

More...
DIPi
DIP-9520N

Protein interaction database and analysis system

More...
IntActi
P0A9B6, 2 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b2927

<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

1339
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
P0A9B6

Database of comparative protein structure models

More...
ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0A9B6

<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>Regioni154 – 156Substrate bindingSequence analysis3
Regioni213 – 214Substrate bindingSequence analysis2

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C17 Bacteria
COG0057 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000071679

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A9B6

KEGG Orthology (KO)

More...
KOi
K03472

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A9B6

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_01640 E4P_dehydrog, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006422 E4P_DH_bac
IPR020831 GlycerAld/Erythrose_P_DH
IPR020830 GlycerAld_3-P_DH_AS
IPR020829 GlycerAld_3-P_DH_cat
IPR020828 GlycerAld_3-P_DH_NAD(P)-bd
IPR036291 NAD(P)-bd_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02800 Gp_dh_C, 1 hit
PF00044 Gp_dh_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000149 GAP_DH, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00078 G3PDHDRGNASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00846 Gp_dh_N, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735 SSF51735, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01532 E4PD_g-proteo, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00071 GAPDH, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0A9B6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTVRVAINGF GRIGRNVVRA LYESGRRAEI TVVAINELAD AAGMAHLLKY
60 70 80 90 100
DTSHGRFAWE VRQERDQLFV GDDAIRVLHE RSLQSLPWRE LGVDVVLDCT
110 120 130 140 150
GVYGSREHGE AHIAAGAKKV LFSHPGSNDL DATVVYGVNQ DQLRAEHRIV
160 170 180 190 200
SNASCTTNCI IPVIKLLDDA YGIESGTVTT IHSAMHDQQV IDAYHPDLRR
210 220 230 240 250
TRAASQSIIP VDTKLAAGIT RFFPQFNDRF EAIAVRVPTI NVTAIDLSVT
260 270 280 290 300
VKKPVKANEV NLLLQKAAQG AFHGIVDYTE LPLVSVDFNH DPHSAIVDGT
310 320 330
QTRVSGAHLI KTLVWCDNEW GFANRMLDTT LAMATVAFR
Length:339
Mass (Da):37,299
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:i4CFC4BD2267EA2A2
GO

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Molecular mass is 37170 Da from positions 2 - 339. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X14436 Genomic DNA Translation: CAA32603.1
U28377 Genomic DNA Translation: AAA69094.1
U00096 Genomic DNA Translation: AAC75964.1
AP009048 Genomic DNA Translation: BAE76991.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S04732 DEECGB

NCBI Reference Sequences

More...
RefSeqi
NP_417402.1, NC_000913.3
WP_000218480.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75964; AAC75964; b2927
BAE76991; BAE76991; BAE76991

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
947413

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2894
eco:b2927

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.3805

<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
X14436 Genomic DNA Translation: CAA32603.1
U28377 Genomic DNA Translation: AAA69094.1
U00096 Genomic DNA Translation: AAC75964.1
AP009048 Genomic DNA Translation: BAE76991.1
PIRiS04732 DEECGB
RefSeqiNP_417402.1, NC_000913.3
WP_000218480.1, NZ_LN832404.1

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
2X5JX-ray2.30O/P/Q/R1-339[»]
2X5KX-ray2.37O/P/Q/R1-339[»]
2XF8X-ray2.95A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P2-339[»]
SMRiP0A9B6
ModBaseiSearch...

Protein-protein interaction databases

BioGridi4262067, 12 interactors
DIPiDIP-9520N
IntActiP0A9B6, 2 interactors
STRINGi511145.b2927

Proteomic databases

jPOSTiP0A9B6
PaxDbiP0A9B6
PRIDEiP0A9B6

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75964; AAC75964; b2927
BAE76991; BAE76991; BAE76991
GeneIDi947413
KEGGiecj:JW2894
eco:b2927
PATRICifig|1411691.4.peg.3805

Organism-specific databases

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

More...
EchoBASEi
EB0363
EcoGeneiEG10368 epd

Phylogenomic databases

eggNOGiENOG4105C17 Bacteria
COG0057 LUCA
HOGENOMiHOG000071679
InParanoidiP0A9B6
KOiK03472
PhylomeDBiP0A9B6

Enzyme and pathway databases

UniPathwayiUPA00244;UER00309
BioCyciEcoCyc:ERYTH4PDEHYDROG-MONOMER
ECOL316407:JW2894-MONOMER
MetaCyc:ERYTH4PDEHYDROG-MONOMER
BRENDAi1.2.1.72 2026
SABIO-RKiP0A9B6

Miscellaneous databases

EvolutionaryTraceiP0A9B6

Protein Ontology

More...
PROi
PR:P0A9B6

Family and domain databases

HAMAPiMF_01640 E4P_dehydrog, 1 hit
InterProiView protein in InterPro
IPR006422 E4P_DH_bac
IPR020831 GlycerAld/Erythrose_P_DH
IPR020830 GlycerAld_3-P_DH_AS
IPR020829 GlycerAld_3-P_DH_cat
IPR020828 GlycerAld_3-P_DH_NAD(P)-bd
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF02800 Gp_dh_C, 1 hit
PF00044 Gp_dh_N, 1 hit
PIRSFiPIRSF000149 GAP_DH, 1 hit
PRINTSiPR00078 G3PDHDRGNASE
SMARTiView protein in SMART
SM00846 Gp_dh_N, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR01532 E4PD_g-proteo, 1 hit
PROSITEiView protein in PROSITE
PS00071 GAPDH, 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 nameiE4PD_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: P0A9B6
Secondary accession number(s): P11603, Q2M9R5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: May 8, 2019
This is version 112 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, Complete proteome, Direct protein sequencing, Reference proteome

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
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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