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Entry version 116 (02 Dec 2020)
Sequence version 1 (08 Nov 2005)
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Protein

Hydroxyacylglutathione hydrolase GloB

Gene

gloB

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

Type II glyoxalase that catalyzes the hydrolysis of (R)-S-lactoylglutathione to (R)-lactate and glutathione (PubMed:25670698, PubMed:17196158). Is more efficient than the isozyme GloC, and plays a major contribution to methylglyoxal (MG) detoxification in E.coli (PubMed:25670698). The two isoenzymes have additive effects and ensure maximal MG degradation (PubMed:25670698).2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

Zn2+1 Publication1 PublicationNote: Binds 2 Zn2+ ions per subunit. Mn2+ and Co2+ can substitute for zinc in reconstitution experiments.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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

Is inhibited by Cu2+.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

kcat is 53 sec(-1) for the hydrolysis of (R)-S-lactoylglutathione (PubMed:17196158). kcat is 15.6 sec(-1) for the hydrolysis of (R)-S-lactoylglutathione (PubMed:25670698).2 Publications
  1. KM=184 µM for (R)-S-lactoylglutathione1 Publication
  2. KM=0.5 mM for (R)-S-lactoylglutathione1 Publication
  1. Vmax=112 µmol/min/mg enzyme for the hydrolysis of (R)-S-lactoylglutathione1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: methylglyoxal degradation

This protein is involved in step 2 of the subpathway that synthesizes (R)-lactate from methylglyoxal.1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Lactoylglutathione lyase (gloA), Lactoylglutathione lyase (gloA)
  2. Hydroxyacylglutathione hydrolase (gloB), Hydroxyacylglutathione hydrolase GloB (gloB), Hydroxyacylglutathione hydrolase GloC (gloC)
This subpathway is part of the pathway methylglyoxal degradation, which is itself part of Secondary metabolite metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (R)-lactate from methylglyoxal, the pathway methylglyoxal degradation and in Secondary metabolite metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi53Zinc 1; via tele nitrogenBy similarity1
Metal bindingi55Zinc 1; via pros nitrogenBy similarity1
Metal bindingi57Zinc 2By similarity1
Metal bindingi58Zinc 2; via tele nitrogenBy similarity1
Metal bindingi110Zinc 1; via tele nitrogenBy similarity1
Metal bindingi127Zinc 1By similarity1
Metal bindingi127Zinc 2By similarity1
Metal bindingi165Zinc 2; via tele nitrogenBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
Biological processDetoxification
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.2.6, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P0AC84

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

More...
UniPathwayi
UPA00619;UER00676

<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%5Fand%5Ftaxonomy%5Fsection">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:
Hydroxyacylglutathione hydrolase GloB2 Publications (EC:3.1.2.62 Publications)
Alternative name(s):
Glyoxalase II2 Publications
Short name:
Glx II2 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:gloB1 Publication
Synonyms:yafR
Ordered Locus Names:b0212, JW0202
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cells lacking this gene show decreased methylglyoxal tolerance. A double deletion mutant lacking both gloB and gloC exhibits almost no resistance to exogenously supplied methylglyoxal, and is unable to grow at MG concentrations as low as 0.1 mM.1 Publication

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001923511 – 251Hydroxyacylglutathione hydrolase GloBAdd BLAST251

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0AC84

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

More...
PaxDbi
P0AC84

PRoteomics IDEntifications database

More...
PRIDEi
P0AC84

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
4262005, 24 interactors

Database of interacting proteins

More...
DIPi
DIP-48248N

Protein interaction database and analysis system

More...
IntActi
P0AC84, 1 interactor

STRING: functional protein association networks

More...
STRINGi
511145.b0212

<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

1251
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P0AC84

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni136 – 138Substrate bindingBy similarity3
Regioni165 – 167Substrate bindingBy similarity3
Regioni245 – 248Substrate bindingBy similarity4

<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
COG0491, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_030571_4_1_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0AC84

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0AC84

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07723, hydroxyacylglutathione_hydrolase_MBL-fold, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.60.15.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01374, Glyoxalase_2, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR035680, Clx_II_MBL
IPR032282, HAGH_C
IPR017782, Hydroxyacylglutathione_Hdrlase
IPR001279, Metallo-B-lactamas
IPR036866, RibonucZ/Hydroxyglut_hydro

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF16123, HAGH_C, 1 hit
PF00753, Lactamase_B, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF005457, Glx, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00849, Lactamase_B, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF56281, SSF56281, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03413, GSH_gloB, 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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

P0AC84-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNLNSIPAFD DNYIWVLNDE AGRCLIVDPG DAEPVLNAIA ANNWQPEAIF
60 70 80 90 100
LTHHHHDHVG GVKELVEKFP QIVVYGPQET QDKGTTQVVK DGETAFVLGH
110 120 130 140 150
EFSVIATPGH TLGHICYFSK PYLFCGDTLF SGGCGRLFEG TASQMYQSLK
160 170 180 190 200
KLSALPDDTL VCCAHEYTLS NMKFALSILP HDLSINDYYR KVKELRAKNQ
210 220 230 240 250
ITLPVILKNE RQINVFLRTE DIDLINVINE ETLLQQPEER FAWLRSKKDR

F
Length:251
Mass (Da):28,434
Last modified:November 8, 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:iD59948B6E12809F5
GO

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

Molecular mass is 28432 Da. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U70214 Genomic DNA Translation: AAB08634.1
U00096 Genomic DNA Translation: AAC73317.1
AP009048 Genomic DNA Translation: BAA77883.1

Protein sequence database of the Protein Information Resource

More...
PIRi
F64745

NCBI Reference Sequences

More...
RefSeqi
NP_414748.1, NC_000913.3
WP_001052715.1, NZ_SSZK01000029.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73317; AAC73317; b0212
BAA77883; BAA77883; BAA77883

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
944902

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0202
eco:b0212

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2072

<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
U70214 Genomic DNA Translation: AAB08634.1
U00096 Genomic DNA Translation: AAC73317.1
AP009048 Genomic DNA Translation: BAA77883.1
PIRiF64745
RefSeqiNP_414748.1, NC_000913.3
WP_001052715.1, NZ_SSZK01000029.1

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
6RZ0X-ray1.10A1-251[»]
6S0IX-ray1.80A1-251[»]
SMRiP0AC84
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4262005, 24 interactors
DIPiDIP-48248N
IntActiP0AC84, 1 interactor
STRINGi511145.b0212

Proteomic databases

jPOSTiP0AC84
PaxDbiP0AC84
PRIDEiP0AC84

Genome annotation databases

EnsemblBacteriaiAAC73317; AAC73317; b0212
BAA77883; BAA77883; BAA77883
GeneIDi944902
KEGGiecj:JW0202
eco:b0212
PATRICifig|1411691.4.peg.2072

Organism-specific databases

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

More...
EchoBASEi
EB3114

Phylogenomic databases

eggNOGiCOG0491, Bacteria
HOGENOMiCLU_030571_4_1_6
InParanoidiP0AC84
PhylomeDBiP0AC84

Enzyme and pathway databases

UniPathwayiUPA00619;UER00676
BioCyciEcoCyc:GLYOXII-MONOMER
MetaCyc:GLYOXII-MONOMER
BRENDAi3.1.2.6, 2026
SABIO-RKiP0AC84

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P0AC84

Family and domain databases

CDDicd07723, hydroxyacylglutathione_hydrolase_MBL-fold, 1 hit
Gene3Di3.60.15.10, 1 hit
HAMAPiMF_01374, Glyoxalase_2, 1 hit
InterProiView protein in InterPro
IPR035680, Clx_II_MBL
IPR032282, HAGH_C
IPR017782, Hydroxyacylglutathione_Hdrlase
IPR001279, Metallo-B-lactamas
IPR036866, RibonucZ/Hydroxyglut_hydro
PfamiView protein in Pfam
PF16123, HAGH_C, 1 hit
PF00753, Lactamase_B, 1 hit
PIRSFiPIRSF005457, Glx, 1 hit
SMARTiView protein in SMART
SM00849, Lactamase_B, 1 hit
SUPFAMiSSF56281, SSF56281, 1 hit
TIGRFAMsiTIGR03413, GSH_gloB, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGLO2_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: P0AC84
Secondary accession number(s): Q47677
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: November 8, 2005
Last modified: December 2, 2020
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, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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