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Protein

3-oxoacyl-[acyl-carrier-protein] reductase FabG

Gene

fabG

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 NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.2 Publications

Miscellaneous

Calcium ions stabilize the structure, and may inhibit FabG activity by obstructing access to the active site.

<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

Inhibited by cinnamic acid derivatives.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>pH dependencei

Optimum pH is between 6.0 and 7.0.1 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: fatty acid biosynthesis

This protein is involved in the pathway fatty acid biosynthesis, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway fatty acid biosynthesis and in Lipid metabolism.

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 sitei37NADPCombined sources1 Publication1
<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 bindingi50Calcium 1; via carbonyl oxygen; shared with dimeric partner1
Metal bindingi53Calcium 1; via carbonyl oxygen; shared with dimeric partner1
Binding sitei86NADP; via carbonyl oxygenCombined sources1 Publication1
Binding sitei138SubstrateBy similarity1
Metal bindingi145Calcium 21
<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 sitei151Proton acceptorPROSITE-ProRule annotation1
Binding sitei184NADP; via amide nitrogen and carbonyl oxygen1 Publication1
Metal bindingi233Calcium 3; shared with dimeric partner1
Metal bindingi234Calcium 3; via carbonyl oxygen; shared with dimeric partner1

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 bindingi12 – 15NADPCombined sources1 Publication4
Nucleotide bindingi59 – 60NADPCombined sources1 Publication2
Nucleotide bindingi151 – 155NADPCombined sources1 Publication5

<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

  • biotin biosynthetic process Source: EcoCyc
  • fatty acid biosynthetic process Source: EcoCyc
  • fatty acid elongation Source: UniProtKB
  • lipid biosynthetic 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 processFatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism
LigandCalcium, Metal-binding, NADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:3-OXOACYL-ACP-REDUCT-MONOMER
MetaCyc:3-OXOACYL-ACP-REDUCT-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
1.1.1.100 2026

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

More...
UniPathwayi
UPA00094

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000853

<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:
3-oxoacyl-[acyl-carrier-protein] reductase FabG (EC:1.1.1.100)
Alternative name(s):
3-ketoacyl-acyl carrier protein reductase
Beta-Ketoacyl-acyl carrier protein reductase
Beta-ketoacyl-ACP reductase
<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:fabG
Ordered Locus Names:b1093, JW1079
<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
EG11318 fabG

<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>Mutagenesisi151Y → F: Defect in the affinity for NADPH. 1 Publication1
Mutagenesisi154A → T: Decreases in the thermolability of the reductase; when associated with K-233. 1 Publication1
Mutagenesisi155K → A: Defect in the affinity for NADPH. 1 Publication1
Mutagenesisi233E → K: Decreases in the thermolability of the reductase; when associated with T-154. 1 Publication1

Chemistry databases

Drug and drug target database

More...
DrugBanki
DB03461 2'-Monophosphoadenosine 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_00000546721 – 2443-oxoacyl-[acyl-carrier-protein] reductase FabGAdd BLAST244

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P0AEK2

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

More...
PaxDbi
P0AEK2

PRoteomics IDEntifications database

More...
PRIDEi
P0AEK2

<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.2 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4260080, 228 interactors

Database of interacting proteins

More...
DIPi
DIP-31869N

Protein interaction database and analysis system

More...
IntActi
P0AEK2, 6 interactors

STRING: functional protein association networks

More...
STRINGi
316385.ECDH10B_1165

<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

1244
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
P0AEK2

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

More...
SMRi
P0AEK2

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
P0AEK2

<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
ENOG4105CHR Bacteria
ENOG410XNW1 LUCA

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0AEK2

KEGG Orthology (KO)

More...
KOi
K00059

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0AEK2

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011284 3oxo_ACP_reduc
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00081 GDHRDH
PR00080 SDRFAMILY

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735 SSF51735, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01830 3oxo_ACP_reduc, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00061 ADH_SHORT, 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.

P0AEK2-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNFEGKIALV TGASRGIGRA IAETLAARGA KVIGTATSEN GAQAISDYLG
60 70 80 90 100
ANGKGLMLNV TDPASIESVL EKIRAEFGEV DILVNNAGIT RDNLLMRMKD
110 120 130 140 150
EEWNDIIETN LSSVFRLSKA VMRAMMKKRH GRIITIGSVV GTMGNGGQAN
160 170 180 190 200
YAAAKAGLIG FSKSLAREVA SRGITVNVVA PGFIETDMTR ALSDDQRAGI
210 220 230 240
LAQVPAGRLG GAQEIANAVA FLASDEAAYI TGETLHVNGG MYMV
Length:244
Mass (Da):25,560
Last modified:December 20, 2005 - v1
<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:i48EC1F2A7F7EEFD9
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 conflicti30A → G in AAA23739 (PubMed:1556094).Curated1
Sequence conflicti43Q → R in AAA23739 (PubMed:1556094).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
M84991 Genomic DNA Translation: AAA23739.1
U00096 Genomic DNA Translation: AAC74177.1
AP009048 Genomic DNA Translation: BAA35901.1
M87040 Genomic DNA Translation: AAA23743.1

Protein sequence database of the Protein Information Resource

More...
PIRi
B64853 B42147

NCBI Reference Sequences

More...
RefSeqi
NP_415611.1, NC_000913.3
WP_001008535.1, NZ_LN832404.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC74177; AAC74177; b1093
BAA35901; BAA35901; BAA35901

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
945645

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW1079
eco:b1093

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.1175

<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
M84991 Genomic DNA Translation: AAA23739.1
U00096 Genomic DNA Translation: AAC74177.1
AP009048 Genomic DNA Translation: BAA35901.1
M87040 Genomic DNA Translation: AAA23743.1
PIRiB64853 B42147
RefSeqiNP_415611.1, NC_000913.3
WP_001008535.1, 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
1I01X-ray2.60A/B/C/D/E/F/G/H1-244[»]
1Q7BX-ray2.05A/B/C/D1-244[»]
1Q7CX-ray2.50A/B1-244[»]
ProteinModelPortaliP0AEK2
SMRiP0AEK2
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260080, 228 interactors
DIPiDIP-31869N
IntActiP0AEK2, 6 interactors
STRINGi316385.ECDH10B_1165

Chemistry databases

DrugBankiDB03461 2'-Monophosphoadenosine 5'-Diphosphoribose
SwissLipidsiSLP:000000853

Proteomic databases

EPDiP0AEK2
PaxDbiP0AEK2
PRIDEiP0AEK2

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74177; AAC74177; b1093
BAA35901; BAA35901; BAA35901
GeneIDi945645
KEGGiecj:JW1079
eco:b1093
PATRICifig|1411691.4.peg.1175

Organism-specific databases

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

More...
EchoBASEi
EB1294
EcoGeneiEG11318 fabG

Phylogenomic databases

eggNOGiENOG4105CHR Bacteria
ENOG410XNW1 LUCA
InParanoidiP0AEK2
KOiK00059
PhylomeDBiP0AEK2

Enzyme and pathway databases

UniPathwayi
UPA00094

BioCyciEcoCyc:3-OXOACYL-ACP-REDUCT-MONOMER
MetaCyc:3-OXOACYL-ACP-REDUCT-MONOMER
BRENDAi1.1.1.100 2026

Miscellaneous databases

EvolutionaryTraceiP0AEK2

Protein Ontology

More...
PROi
PR:P0AEK2

Family and domain databases

InterProiView protein in InterPro
IPR011284 3oxo_ACP_reduc
IPR036291 NAD(P)-bd_dom_sf
IPR020904 Sc_DH/Rdtase_CS
IPR002347 SDR_fam
PRINTSiPR00081 GDHRDH
PR00080 SDRFAMILY
SUPFAMiSSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR01830 3oxo_ACP_reduc, 1 hit
PROSITEiView protein in PROSITE
PS00061 ADH_SHORT, 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 nameiFABG_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: P0AEK2
Secondary accession number(s): P25716, P78221, Q47202
<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: December 20, 2005
Last sequence update: December 20, 2005
Last modified: December 5, 2018
This is version 116 of the entry and version 1 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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