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UniProtKB - P0A759 (NAGB_ECOLI)

Entry version 130 (07 Apr 2021)
Sequence version 1 (07 Jun 2005)
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Protein

Glucosamine-6-phosphate deaminase

Gene

nagB

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 reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.

Miscellaneous

Disulfide bonds seem not to be essential for the stability of the oligomer under physiological conditions.

<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 <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

Allosterically activated by N-acetylglucosamine 6-phosphate (GlcNAc6P). Competitively inhibited by 2-amino-2-deoxy-D-glucitol-6-phosphate (GlcN-ol-6P).

<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: N-acetylneuraminate degradation

This protein is involved in step 5 of the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. N-acetylneuraminate lyase (nanA), N-acetylneuraminate lyase (nanA)
  2. N-acetylmannosamine kinase (nanK), N-acetylmannosamine kinase (nanK)
  3. Putative N-acetylmannosamine-6-phosphate 2-epimerase (nanE), Putative N-acetylmannosamine-6-phosphate 2-epimerase (nanE)
  4. N-acetylglucosamine-6-phosphate deacetylase (nagA)
  5. Glucosamine-6-phosphate deaminase (nagB), Glucosamine-6-phosphate deaminase (nagB)
This subpathway is part of the pathway N-acetylneuraminate degradation, which is itself part of Amino-sugar metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-fructose 6-phosphate from N-acetylneuraminate, the pathway N-acetylneuraminate degradation and in Amino-sugar metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei72Proton acceptor; for enolization step1 Publication1
Active sitei141For ring-opening step1 Publication1
Active sitei143Proton acceptor; for ring-opening step1 Publication1
Active sitei148For ring-opening step1 Publication1
<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>Sitei151Part of the allosteric site1
Sitei158Part of the allosteric site1
Sitei160Part of the allosteric site1
Sitei161Part of the allosteric site1
Sitei254Part of the allosteric site1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionAllosteric enzyme, Hydrolase
Biological processCarbohydrate metabolism

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:GLUCOSAMINE-6-P-DEAMIN-MONOMER
MetaCyc:GLUCOSAMINE-6-P-DEAMIN-MONOMER

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.5.99.6, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P0A759

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

More...UniPathwayi		UPA00629;UER00684

<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:
Glucosamine-6-phosphate deaminase (EC:3.5.99.6)
Alternative name(s):
GlcN6P deaminase
Short name:
GNPDA
Glucosamine-6-phosphate isomerase
<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:nagB
Synonyms:glmD
Ordered Locus Names:b0678, JW0664
<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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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 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

<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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi118C → S: 50% of wild-type activity, but 2-fold decrease in substrate affinity. 1 Publication1
Mutagenesisi141D → N: Large decrease in activity. 1 Publication1
Mutagenesisi143H → Q: Loss of activity for the deamination reaction but not for the reverse reaction; complete loss of the homotropic cooperativity. 1 Publication1
Mutagenesisi148E → Q: Large decrease in activity. 1 Publication1
Mutagenesisi174F → A: Loss of activity in the absence of the allosteric activator. 1
Mutagenesisi239C → S: 50% of wild-type activity, but 2-fold decrease in substrate affinity; decrease in allosteric interaction energy. 1 Publication1

Chemistry databases

Drug and drug target database

More...DrugBanki		DB02445, 2-Deoxy-2-Amino Glucitol-6-Phosphate
DB03951, N-acetyl-D-glucosamine-6-phosphate

<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_00001601431 – 266Glucosamine-6-phosphate deaminaseAdd BLAST266

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi219Interchain1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0A759

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

More...PaxDbi		P0A759

PRoteomics IDEntifications database

More...PRIDEi		P0A759

<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

Homohexamer; trimer of disulfide-linked dimers.

1 Publication

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4261792, 32 interactors

Database of interacting proteins

More...DIPi		DIP-35992N

Protein interaction database and analysis system

More...IntActi		P0A759, 11 interactors

STRING: functional protein association networks

More...STRINGi		511145.b0678

<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

1266
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		P0A759

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P0A759

<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 glucosamine/galactosamine-6-phosphate isomerase family. NagB subfamily.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG0363, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_049611_0_1_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P0A759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P0A759

Family and domain databases

Conserved Domains Database

More...CDDi		cd01399, GlcN6P_deaminase, 1 hit

HAMAP database of protein families

More...HAMAPi		MF_01241, GlcN6P_deamin, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR006148, Glc/Gal-6P_isomerase
IPR004547, Glucosamine6P_isomerase
IPR018321, Glucosamine6P_isomerase_CS
IPR037171, NagB/RpiA_transferase-like

The PANTHER Classification System

More...PANTHERi		PTHR11280, PTHR11280, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01182, Glucosamine_iso, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF100950, SSF100950, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00502, nagB, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS01161, GLC_GALNAC_ISOMERASE, 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.

P0A759-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRLIPLTTAE QVGKWAARHI VNRINAFKPT ADRPFVLGLP TGGTPMTTYK 
        60         70         80         90        100
ALVEMHKAGQ VSFKHVVTFN MDEYVGLPKE HPESYYSFMH RNFFDHVDIP 
       110        120        130        140        150
AENINLLNGN APDIDAECRQ YEEKIRSYGK IHLFMGGVGN DGHIAFNEPA 
       160        170        180        190        200
SSLASRTRIK TLTHDTRVAN SRFFDNDVNQ VPKYALTVGV GTLLDAEEVM 
       210        220        230        240        250
ILVLGSQKAL ALQAAVEGCV NHMWTISCLQ LHPKAIMVCD EPSTMELKVK 
       260 
TLRYFNELEA ENIKGL
Length:266
Mass (Da):29,774
Last modified:June 7, 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:iD1443A40E74AC08E
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 conflicti70N → NM in AAC09324 (PubMed:2190615).Curated1
Sequence conflicti91Missing in AAC09324 (PubMed:2190615).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
M19284 Genomic DNA Translation: AAA24191.1
AF052007 Genomic DNA Translation: AAC09324.1
U00096 Genomic DNA Translation: AAC73772.1
AP009048 Genomic DNA Translation: BAA35321.1

Protein sequence database of the Protein Information Resource

More...PIRi		A29895, MUECNG

NCBI Reference Sequences

More...RefSeqi		NP_415204.1, NC_000913.3
WP_001237072.1, NZ_STEB01000044.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC73772; AAC73772; b0678
BAA35321; BAA35321; BAA35321

Database of genes from NCBI RefSeq genomes

More...GeneIDi		58461678
945290

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW0664
eco:b0678

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.1600

<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
M19284 Genomic DNA Translation: AAA24191.1
AF052007 Genomic DNA Translation: AAC09324.1
U00096 Genomic DNA Translation: AAC73772.1
AP009048 Genomic DNA Translation: BAA35321.1
PIRiA29895, MUECNG
RefSeqiNP_415204.1, NC_000913.3
WP_001237072.1, NZ_STEB01000044.1

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
1CD5X-ray2.30A1-266[»]
1DEAX-ray2.10A/B1-266[»]
1FQOX-ray2.20A/B1-266[»]
1FRZX-ray2.20A/B1-266[»]
1FS5X-ray1.73A/B1-266[»]
1FS6X-ray2.20A1-266[»]
1FSFX-ray1.90A1-266[»]
1HORX-ray2.40A/B1-266[»]
1HOTX-ray2.40A/B1-266[»]
1JT9X-ray2.06A1-266[»]
2WU1X-ray2.20A/B1-266[»]
SMRiP0A759
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261792, 32 interactors
DIPiDIP-35992N
IntActiP0A759, 11 interactors
STRINGi511145.b0678

Chemistry databases

DrugBankiDB02445, 2-Deoxy-2-Amino Glucitol-6-Phosphate
DB03951, N-acetyl-D-glucosamine-6-phosphate

Proteomic databases

jPOSTiP0A759
PaxDbiP0A759
PRIDEiP0A759

Genome annotation databases

EnsemblBacteriaiAAC73772; AAC73772; b0678
BAA35321; BAA35321; BAA35321
GeneIDi58461678
945290
KEGGiecj:JW0664
eco:b0678
PATRICifig|1411691.4.peg.1600

Organism-specific databases

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

More...EchoBASEi		EB0627

Phylogenomic databases

eggNOGiCOG0363, Bacteria
HOGENOMiCLU_049611_0_1_6
InParanoidiP0A759
PhylomeDBiP0A759

Enzyme and pathway databases

UniPathwayiUPA00629;UER00684
BioCyciEcoCyc:GLUCOSAMINE-6-P-DEAMIN-MONOMER
MetaCyc:GLUCOSAMINE-6-P-DEAMIN-MONOMER
BRENDAi3.5.99.6, 2026
SABIO-RKiP0A759

Miscellaneous databases

EvolutionaryTraceiP0A759

Protein Ontology

More...PROi		PR:P0A759

Family and domain databases

CDDicd01399, GlcN6P_deaminase, 1 hit
HAMAPiMF_01241, GlcN6P_deamin, 1 hit
InterProiView protein in InterPro
IPR006148, Glc/Gal-6P_isomerase
IPR004547, Glucosamine6P_isomerase
IPR018321, Glucosamine6P_isomerase_CS
IPR037171, NagB/RpiA_transferase-like
PANTHERiPTHR11280, PTHR11280, 1 hit
PfamiView protein in Pfam
PF01182, Glucosamine_iso, 1 hit
SUPFAMiSSF100950, SSF100950, 1 hit
TIGRFAMsiTIGR00502, nagB, 1 hit
PROSITEiView protein in PROSITE
PS01161, GLC_GALNAC_ISOMERASE, 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 nameiNAGB_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: P0A759
Secondary accession number(s): O68603, P09375
<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: June 7, 2005
Last sequence update: June 7, 2005
Last modified: April 7, 2021
This is version 130 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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