Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

GDP-mannose mannosyl hydrolase

Gene

gmm

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

Hydrolyzes both GDP-mannose and GDP-glucose. Could participate in the regulation of cell wall biosynthesis by influencing the concentration of GDP-mannose or GDP-glucose in the cell. Might also be involved in the biosynthesis of the slime polysaccharide colanic acid.2 Publications

<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+UniRule annotation3 PublicationsNote: Binds 1 Mg2+ ion per subunit.UniRule annotation3 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

GDP-alpha-D-mannose is likely to be the biological substrate, but the Kcat/KM obtained with GDP-alpha-D-glucose is very similar to that with GDP-alpha-D-mannose.
  1. KM=0.3 mM for GDP-mannose1 Publication
  2. KM=1.9 mM for GDP-glucose1 Publication
  1. Vmax=1.6 µmol/min/mg enzyme with GDP-mannose as substrate1 Publication
  2. Vmax=7.5 µmol/min/mg enzyme with GDP-glucose as substrate1 Publication

pH dependencei

Optimum pH is 9.3.1 Publication

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 sitei8SubstrateUniRule annotation2 Publications1
Binding sitei36SubstrateUniRule annotation2 Publications1
<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 bindingi49Magnesium; via carbonyl oxygenUniRule annotation2 Publications1
Metal bindingi69MagnesiumUniRule annotation2 Publications1
Metal bindingi122MagnesiumUniRule annotation2 Publications1
<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>Sitei123Critical for catalysis1

<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

  • GDP-glucosidase activity Source: EcoCyc
  • GDP-mannose mannosyl hydrolase activity Source: UniProtKB-UniRule
  • magnesium ion binding Source: EcoCyc
  • manganese ion binding Source: EcoCyc

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 functionHydrolase
Biological processLipopolysaccharide biosynthesis
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P32056

<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:
GDP-mannose mannosyl hydrolaseUniRule annotation (EC:3.6.1.-UniRule annotation)
Short name:
GDPMHUniRule annotation
Alternative name(s):
Colanic acid biosynthesis protein WcaH
<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:gmmUniRule annotation
Synonyms:nudD, wcaH, yefC
Ordered Locus Names:b2051, JW5335
<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
EG11789 gmm

<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>Mutagenesisi21D → A: Increases Km for GDP-mannose 5-fold. Reduces activity 120-fold. 1 Publication1
Mutagenesisi21D → N: Increases Km for GDP-mannose 9-fold. Reduces activity 400-fold. 1 Publication1
Mutagenesisi36R → Q: Increases Km for GDP-mannose 9-fold. Reduces activity 24-fold. 1 Publication1
Mutagenesisi51R → K: Increases Km for GDP-mannose 40-fold. Reduces activity 10-fold. 1 Publication1
Mutagenesisi51R → Q: Increases Km for GDP-mannose 40-fold. Reduces activity 300-fold. 1 Publication1
Mutagenesisi64R → Q: Increases Km for GDP-mannose 80-fold. Reduces activity 24-fold. 1 Publication1
Mutagenesisi69E → Q: Increases Km for GDP-mannose 10-fold. Increases Km for magnesium 40-fold. Reduces activity 150-fold. 1
Mutagenesisi87H → Q: Increases Km for GDP-mannose 4-fold. Reduces activity 200-fold. 1 Publication1
Mutagenesisi101H → Q: Increases Km for GDP-mannose 14-fold. Reduces activity 7-fold. 1 Publication1
Mutagenesisi102Y → F: Increases Km for GDP-mannose 7-fold. Reduces activity 100-fold. 1 Publication1
Mutagenesisi123H → Q: Increases Km for GDP-mannose 5-fold. Reduces activity 2000-fold. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB04315 Guanosine-5'-Diphosphate

<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_00000569831 – 159GDP-mannose mannosyl hydrolaseAdd BLAST159

Proteomic databases

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

More...
PaxDbi
P32056

PRoteomics IDEntifications database

More...
PRIDEi
P32056

<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.UniRule annotation3 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4261145, 369 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_2201

<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

1159
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P32056

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

More...
SMRi
P32056

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P32056

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini13 – 153Nudix hydrolaseUniRule annotationAdd BLAST141

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>Regioni2 – 3Substrate binding2

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi50 – 71Nudix boxAdd BLAST22

<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 Nudix hydrolase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105FGF Bacteria
COG0494 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000280400

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P32056

KEGG Orthology (KO)

More...
KOi
K03207

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P32056

Family and domain databases

Conserved Domains Database

More...
CDDi
cd03430 GDPMH, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00941 GDPMH_gmm, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR033715 GDPMH
IPR028613 GDPMH_Gmm
IPR015797 NUDIX_hydrolase-like_dom_sf
IPR020084 NUDIX_hydrolase_CS
IPR000086 NUDIX_hydrolase_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00293 NUDIX, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF037599 GDPMH, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF55811 SSF55811, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51462 NUDIX, 1 hit
PS00893 NUDIX_BOX, 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.

P32056-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFLRQEDFAT VVRSTPLVSL DFIVENSRGE FLLGKRTNRP AQGYWFVPGG
60 70 80 90 100
RVQKDETLEA AFERLTMAEL GLRLPITAGQ FYGVWQHFYD DNFSGTDFTT
110 120 130 140 150
HYVVLGFRFR VSEEELLLPD EQHDDYRWLT SDALLASDNV HANSRAYFLA

EKRTGVPGL
Length:159
Mass (Da):18,273
Last modified:March 27, 2002 - 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:iC7ADFFC56AD6B32A
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAC77844 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

<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 18472±67 Da from positions 1 - 159. Determined by MALDI. 1 Publication

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
U38473 Genomic DNA Translation: AAC77844.1 Different initiation.
U00096 Genomic DNA Translation: AAC75112.2
AP009048 Genomic DNA Translation: BAA15907.2

Protein sequence database of the Protein Information Resource

More...
PIRi
E55239

NCBI Reference Sequences

More...
RefSeqi
NP_416555.2, NC_000913.3
WP_001393539.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75112; AAC75112; b2051
BAA15907; BAA15907; BAA15907

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
946559

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW5335
eco:b2051

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|511145.12.peg.2128

<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
U38473 Genomic DNA Translation: AAC77844.1 Different initiation.
U00096 Genomic DNA Translation: AAC75112.2
AP009048 Genomic DNA Translation: BAA15907.2
PIRiE55239
RefSeqiNP_416555.2, NC_000913.3
WP_001393539.1, 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
1RYAX-ray1.30A/B1-159[»]
2GT2X-ray2.00A/B/C/D1-159[»]
2GT4X-ray2.30A/B/C1-159[»]
ProteinModelPortaliP32056
SMRiP32056
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261145, 369 interactors
STRINGi316385.ECDH10B_2201

Chemistry databases

DrugBankiDB04315 Guanosine-5'-Diphosphate

Proteomic databases

PaxDbiP32056
PRIDEiP32056

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75112; AAC75112; b2051
BAA15907; BAA15907; BAA15907
GeneIDi946559
KEGGiecj:JW5335
eco:b2051
PATRICifig|511145.12.peg.2128

Organism-specific databases

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

More...
EchoBASEi
EB1737
EcoGeneiEG11789 gmm

Phylogenomic databases

eggNOGiENOG4105FGF Bacteria
COG0494 LUCA
HOGENOMiHOG000280400
InParanoidiP32056
KOiK03207
PhylomeDBiP32056

Enzyme and pathway databases

BioCyciEcoCyc:GDPMANMANHYDRO-MONOMER
MetaCyc:GDPMANMANHYDRO-MONOMER
SABIO-RKiP32056

Miscellaneous databases

EvolutionaryTraceiP32056

Protein Ontology

More...
PROi
PR:P32056

Family and domain databases

CDDicd03430 GDPMH, 1 hit
HAMAPiMF_00941 GDPMH_gmm, 1 hit
InterProiView protein in InterPro
IPR033715 GDPMH
IPR028613 GDPMH_Gmm
IPR015797 NUDIX_hydrolase-like_dom_sf
IPR020084 NUDIX_hydrolase_CS
IPR000086 NUDIX_hydrolase_dom
PfamiView protein in Pfam
PF00293 NUDIX, 1 hit
PIRSFiPIRSF037599 GDPMH, 1 hit
SUPFAMiSSF55811 SSF55811, 1 hit
PROSITEiView protein in PROSITE
PS51462 NUDIX, 1 hit
PS00893 NUDIX_BOX, 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 nameiGMM_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: P32056
<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, 1993
Last sequence update: March 27, 2002
Last modified: December 5, 2018
This is version 139 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, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again