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Protein

GDP-L-fucose synthase

Gene

fcl

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 two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction.UniRule annotation3 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 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

Subject to product inhibition by NADP and GDP-fucose.1 Publication

<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=9 µM for NADPH2 Publications
  2. KM=109 µM for NADH2 Publications
  3. KM=29 µM for GDP-4-keto-6-deoxymannose2 Publications
  1. Vmax=363.5 µmol/min/mg enzyme2 Publications

pH dependencei

Optimum pH is 6-6.5.2 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: GDP-L-fucose biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes GDP-L-fucose from GDP-alpha-D-mannose.UniRule annotation1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. GDP-mannose 4,6-dehydratase (gmd)
  2. GDP-L-fucose synthase (fcl)
This subpathway is part of the pathway GDP-L-fucose biosynthesis via de novo pathway, which is itself part of Nucleotide-sugar biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes GDP-L-fucose from GDP-alpha-D-mannose, the pathway GDP-L-fucose biosynthesis via de novo pathway and in Nucleotide-sugar biosynthesis.

Pathwayi: colanic acid biosynthesis

This protein is involved in the pathway colanic acid biosynthesis, which is part of Exopolysaccharide biosynthesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway colanic acid biosynthesis and in Exopolysaccharide biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei107Important for catalytic activity1
Sitei109Important for catalytic activity1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei136Proton donor/acceptorUniRule annotation1 Publication1
<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 sitei140NADPUniRule annotation3 Publications1
Sitei140Lowers pKa of active site Tyr1
Binding sitei179NADPUniRule annotation3 Publications1
Binding sitei187SubstrateCurated1
Binding sitei202SubstrateUniRule annotation1
Binding sitei209SubstrateUniRule annotation1
Binding sitei278SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi10 – 16NADPUniRule annotation3 Publications7
Nucleotide bindingi36 – 41NADPUniRule annotation3 Publications6
Nucleotide bindingi105 – 108NADPUniRule annotation3 Publications4
Nucleotide bindingi163 – 166NADPUniRule annotation3 Publications4

<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-L-fucose synthase activity Source: EcoCyc
  • isomerase activity Source: UniProtKB-KW
  • NADP+ binding Source: UniProtKB-UniRule

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 functionIsomerase, Multifunctional enzyme, Oxidoreductase
LigandNADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.1.271 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P32055

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

More...
UniPathwayi
UPA00128;UER00191

UPA00980

<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-L-fucose synthaseUniRule annotation (EC:1.1.1.271UniRule annotation3 Publications)
Alternative name(s):
GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductaseUniRule annotation
<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:fclUniRule annotation
Synonyms:wcaG, yefB
Ordered Locus Names:b2052, JW2037
<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
EG11788 fcl

<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>Mutagenesisi107S → A: Nearly abolishes catalytic activity. Minor effect of affinity for NADPH and substrate. 1 Publication1
Mutagenesisi109C → A: Nearly abolishes catalytic activity. 1
Mutagenesisi136Y → E: Abolishes enzyme activity. 1 Publication1
Mutagenesisi140K → R: Reduces catalytic activity 20-fold. 1 Publication1
Mutagenesisi140K → S: Nearly abolishes catalytic activity. 1 Publication1
Mutagenesisi179H → N: Nearly abolishes catalytic activity. 1 Publication1
Mutagenesisi187R → A: Decreases affinity for the substrate GDP-4-keto-6-deoxymannose. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
DB02897 Acetylphosphate

<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_00001743581 – 321GDP-L-fucose synthaseAdd BLAST321

Proteomic databases

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

More...
PaxDbi
P32055

PRoteomics IDEntifications database

More...
PRIDEi
P32055

<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.3 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4259691, 221 interactors

Protein interaction database and analysis system

More...
IntActi
P32055, 2 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_2202

<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

1321
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
P32055

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

More...
SMRi
P32055

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
P32055

<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

<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 NAD(P)-dependent epimerase/dehydratase family. Fucose synthase subfamily.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C30 Bacteria
COG0451 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000168011

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P32055

KEGG Orthology (KO)

More...
KOi
K02377

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P32055

Family and domain databases

Conserved Domains Database

More...
CDDi
cd05239 GDP_FS_SDR_e, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00956 GDP_fucose_synth, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001509 Epimerase_deHydtase
IPR028614 GDP_fucose/colitose_synth
IPR036291 NAD(P)-bd_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01370 Epimerase, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735 SSF51735, 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.

P32055-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKQRVFIAG HRGMVGSAIR RQLEQRGDVE LVLRTRDELN LLDSRAVHDF
60 70 80 90 100
FASERIDQVY LAAAKVGGIV ANNTYPADFI YQNMMIESNI IHAAHQNDVN
110 120 130 140 150
KLLFLGSSCI YPKLAKQPMA ESELLQGTLE PTNEPYAIAK IAGIKLCESY
160 170 180 190 200
NRQYGRDYRS VMPTNLYGPH DNFHPSNSHV IPALLRRFHE ATAQNAPDVV
210 220 230 240 250
VWGSGTPMRE FLHVDDMAAA SIHVMELAHE VWLENTQPML SHINVGTGVD
260 270 280 290 300
CTIRELAQTI AKVVGYKGRV VFDASKPDGT PRKLLDVTRL HQLGWYHEIS
310 320
LEAGLASTYQ WFLENQDRFR G
Length:321
Mass (Da):36,141
Last modified:November 1, 1997 - 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:i97077193D79684C7
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti255 – 256EL → DV no nucleotide entry (PubMed:7815923).Curated2
Sequence conflicti255 – 256EL → DV in AAC77843 (PubMed:8759852).Curated2

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U38473 Genomic DNA Translation: AAC77843.1
U00096 Genomic DNA Translation: AAC75113.1
AP009048 Genomic DNA Translation: BAA15908.1

Protein sequence database of the Protein Information Resource

More...
PIRi
C64971

NCBI Reference Sequences

More...
RefSeqi
NP_416556.1, NC_000913.3
WP_000043654.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75113; AAC75113; b2052
BAA15908; BAA15908; BAA15908

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
946563

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2037
eco:b2052

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.199

<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: AAC77843.1
U00096 Genomic DNA Translation: AAC75113.1
AP009048 Genomic DNA Translation: BAA15908.1
PIRiC64971
RefSeqiNP_416556.1, NC_000913.3
WP_000043654.1, 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
1BSVX-ray2.20A1-321[»]
1BWSX-ray2.20A1-321[»]
1E6UX-ray1.45A1-321[»]
1E7QX-ray1.60A1-321[»]
1E7RX-ray1.60A1-321[»]
1E7SX-ray1.50A1-321[»]
1FXSX-ray2.30A1-321[»]
1GFSX-ray2.20A1-321[»]
ProteinModelPortaliP32055
SMRiP32055
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259691, 221 interactors
IntActiP32055, 2 interactors
STRINGi316385.ECDH10B_2202

Chemistry databases

DrugBankiDB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
DB02897 Acetylphosphate

Proteomic databases

PaxDbiP32055
PRIDEiP32055

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75113; AAC75113; b2052
BAA15908; BAA15908; BAA15908
GeneIDi946563
KEGGiecj:JW2037
eco:b2052
PATRICifig|1411691.4.peg.199

Organism-specific databases

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

More...
EchoBASEi
EB1736
EcoGeneiEG11788 fcl

Phylogenomic databases

eggNOGiENOG4105C30 Bacteria
COG0451 LUCA
HOGENOMiHOG000168011
InParanoidiP32055
KOiK02377
PhylomeDBiP32055

Enzyme and pathway databases

UniPathwayi
UPA00128;UER00191

UPA00980

BioCyciEcoCyc:FCL-MONOMER
MetaCyc:FCL-MONOMER
BRENDAi1.1.1.271 2026
SABIO-RKiP32055

Miscellaneous databases

EvolutionaryTraceiP32055

Protein Ontology

More...
PROi
PR:P32055

Family and domain databases

CDDicd05239 GDP_FS_SDR_e, 1 hit
HAMAPiMF_00956 GDP_fucose_synth, 1 hit
InterProiView protein in InterPro
IPR001509 Epimerase_deHydtase
IPR028614 GDP_fucose/colitose_synth
IPR036291 NAD(P)-bd_dom_sf
PfamiView protein in Pfam
PF01370 Epimerase, 1 hit
SUPFAMiSSF51735 SSF51735, 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 nameiFCL_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: P32055
Secondary accession number(s): P76382
<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: November 1, 1997
Last modified: December 5, 2018
This is version 156 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
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