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

Lactaldehyde reductase

Gene

fucO

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

<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

Fe cation1 Publication

<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

Inhibited by Zn2+.1 Publication

<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: L-fucose degradation

This protein is involved in the pathway L-fucose degradation, which is part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the pathway L-fucose degradation and in Carbohydrate degradation.

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 sitei38NAD1
Binding sitei70NAD1
Binding sitei150NAD1
Binding sitei161NAD1
<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 bindingi195Iron1
Metal bindingi199Iron; via tele nitrogen1
Metal bindingi262Iron; via tele nitrogen1
Metal bindingi276Iron; via tele nitrogen1

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 bindingi97 – 98NAD2
Nucleotide bindingi139 – 143NAD5
Nucleotide bindingi180 – 184NAD5

<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

  • alcohol dehydrogenase (NAD) activity Source: GO_Central
  • ferrous iron binding Source: EcoCyc
  • lactaldehyde reductase activity Source: EcoCyc

GO - Biological processi

  • glycol catabolic process Source: EcoCyc
  • L-fucose catabolic process Source: EcoCyc
  • propanediol metabolic process Source: EcoCyc
  • rhamnose catabolic process 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 functionOxidoreductase
Biological processCarbohydrate metabolism, Fucose metabolism
LigandIron, Metal-binding, NAD

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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

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

More...
UniPathwayi
UPA00563

<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:
Lactaldehyde reductase (EC:1.1.1.77)
Alternative name(s):
Propanediol oxidoreductase
<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:fucO
Ordered Locus Names:b2799, JW2770
<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
EG10351 fucO

<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

<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>Mutagenesisi1 – 9MANRMILNE → M: Loss of enzyme activity, loss of dimerization. 1 Publication9
Mutagenesisi16G → D: No effect on enzyme activity. 1 Publication1
Mutagenesisi38D → G: Enzyme can now use NADP. 1 Publication1
Mutagenesisi96G → E: Loss of NAD binding and enzyme activity. 1 Publication1
Mutagenesisi195D → L: Complete loss of iron-binding. 1 Publication1
Mutagenesisi199H → A or F: Complete loss of iron-binding. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB02059 Adenosine-5-Diphosphoribose

<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_00000878241 – 382Lactaldehyde reductaseAdd BLAST382

Proteomic databases

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

More...
PaxDbi
P0A9S1

PRoteomics IDEntifications database

More...
PRIDEi
P0A9S1

<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.1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4259223, 91 interactors

Database of interacting proteins

More...
DIPi
DIP-48076N

Protein interaction database and analysis system

More...
IntActi
P0A9S1, 5 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_2968

<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

1382
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
P0A9S1

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

More...
SMRi
P0A9S1

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
P0A9S1

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105C0A Bacteria
COG1454 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000243333

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A9S1

KEGG Orthology (KO)

More...
KOi
K00048

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001670 ADH_Fe/GldA
IPR018211 ADH_Fe_CS
IPR039697 Alcohol_dehydrogenase_Fe
IPR013460 Lactal_redase

The PANTHER Classification System

More...
PANTHERi
PTHR11496 PTHR11496, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00465 Fe-ADH, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02638 lactal_redase, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00913 ADH_IRON_1, 1 hit
PS00060 ADH_IRON_2, 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.

P0A9S1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MANRMILNET AWFGRGAVGA LTDEVKRRGY QKALIVTDKT LVQCGVVAKV
60 70 80 90 100
TDKMDAAGLA WAIYDGVVPN PTITVVKEGL GVFQNSGADY LIAIGGGSPQ
110 120 130 140 150
DTCKAIGIIS NNPEFADVRS LEGLSPTNKP SVPILAIPTT AGTAAEVTIN
160 170 180 190 200
YVITDEEKRR KFVCVDPHDI PQVAFIDADM MDGMPPALKA ATGVDALTHA
210 220 230 240 250
IEGYITRGAW ALTDALHIKA IEIIAGALRG SVAGDKDAGE EMALGQYVAG
260 270 280 290 300
MGFSNVGLGL VHGMAHPLGA FYNTPHGVAN AILLPHVMRY NADFTGEKYR
310 320 330 340 350
DIARVMGVKV EGMSLEEARN AAVEAVFALN RDVGIPPHLR DVGVRKEDIP
360 370 380
ALAQAALDDV CTGGNPREAT LEDIVELYHT AW
Length:382
Mass (Da):40,513
Last modified:November 16, 2011 - 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:iE4D927AC8142098B
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 AAA23824 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAA23825 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB40449 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence BAE76871 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence CAA33124 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

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 conflicti273N → T in CAA33124 (PubMed:2664711).Curated1

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
M31059 Genomic DNA Translation: AAA23824.1 Different initiation.
X15025 Genomic DNA Translation: CAA33124.1 Different initiation.
M27177 Genomic DNA Translation: AAA23825.1 Different initiation.
U29581 Genomic DNA Translation: AAB40449.1 Different initiation.
U00096 Genomic DNA Translation: AAC75841.2
AP009048 Genomic DNA Translation: BAE76871.1 Different initiation.
L07763 Genomic DNA No translation available.

Protein sequence database of the Protein Information Resource

More...
PIRi
A32883 RDECLA

NCBI Reference Sequences

More...
RefSeqi
NP_417279.2, NC_000913.3
WP_000013588.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC75841; AAC75841; b2799
BAE76871; BAE76871; BAE76871

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
947273

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW2770
eco:b2799

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.3934

<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
M31059 Genomic DNA Translation: AAA23824.1 Different initiation.
X15025 Genomic DNA Translation: CAA33124.1 Different initiation.
M27177 Genomic DNA Translation: AAA23825.1 Different initiation.
U29581 Genomic DNA Translation: AAB40449.1 Different initiation.
U00096 Genomic DNA Translation: AAC75841.2
AP009048 Genomic DNA Translation: BAE76871.1 Different initiation.
L07763 Genomic DNA No translation available.
PIRiA32883 RDECLA
RefSeqiNP_417279.2, NC_000913.3
WP_000013588.1, 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
1RRMX-ray1.60A/B1-382[»]
2BI4X-ray2.85A/B1-382[»]
2BL4X-ray2.85A/B1-382[»]
5BR4X-ray0.91A/B1-382[»]
ProteinModelPortaliP0A9S1
SMRiP0A9S1
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259223, 91 interactors
DIPiDIP-48076N
IntActiP0A9S1, 5 interactors
STRINGi316385.ECDH10B_2968

Chemistry databases

DrugBankiDB02059 Adenosine-5-Diphosphoribose

Proteomic databases

PaxDbiP0A9S1
PRIDEiP0A9S1

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75841; AAC75841; b2799
BAE76871; BAE76871; BAE76871
GeneIDi947273
KEGGiecj:JW2770
eco:b2799
PATRICifig|1411691.4.peg.3934

Organism-specific databases

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

More...
EchoBASEi
EB0347
EcoGeneiEG10351 fucO

Phylogenomic databases

eggNOGiENOG4105C0A Bacteria
COG1454 LUCA
HOGENOMiHOG000243333
InParanoidiP0A9S1
KOiK00048

Enzyme and pathway databases

UniPathwayi
UPA00563

BioCyciEcoCyc:LACTALDREDUCT-MONOMER
MetaCyc:LACTALDREDUCT-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A9S1

Protein Ontology

More...
PROi
PR:P0A9S1

Family and domain databases

InterProiView protein in InterPro
IPR001670 ADH_Fe/GldA
IPR018211 ADH_Fe_CS
IPR039697 Alcohol_dehydrogenase_Fe
IPR013460 Lactal_redase
PANTHERiPTHR11496 PTHR11496, 1 hit
PfamiView protein in Pfam
PF00465 Fe-ADH, 1 hit
TIGRFAMsiTIGR02638 lactal_redase, 1 hit
PROSITEiView protein in PROSITE
PS00913 ADH_IRON_1, 1 hit
PS00060 ADH_IRON_2, 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 nameiFUCO_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: P0A9S1
Secondary accession number(s): P11549, Q2MA35
<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: November 16, 2011
Last modified: December 5, 2018
This is version 103 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
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