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UniProtKB - P09148 (GAL7_ECOLI)

Entry version 180 (07 Apr 2021)
Sequence version 2 (01 Nov 1997)
Previous versions | rss
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Protein

Galactose-1-phosphate uridylyltransferase

Gene

galT

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

Miscellaneous

Iron binding is not required for protein folding or enzyme activity.1 Publication

<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+3 PublicationsNote: Binds 1 zinc ion per subunit. Zinc binding seems to play a structural role.3 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.200 mM for uridine 5'-diphosphate glucose1 Publication
  2. KM=0.303 mM for galactose-1-phosphate1 Publication
  3. KM=0.121 mM for uridine 5'-diphosphate galactose1 Publication
  4. KM=0.157 mM for glucose-1-phosphate1 Publication
  1. Vmax=180 µmol/min/mg enzyme1 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: galactose metabolism

This protein is involved in the pathway galactose metabolism, which is part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the pathway galactose metabolism and in Carbohydrate 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 bindingi52ZincCombined sources2 Publications1
Metal bindingi55ZincCombined sources2 Publications1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei61UDP-alpha-D-glucose; via amide nitrogenCombined sources1 Publication1
Metal bindingi115ZincCombined sources2 Publications1
Binding sitei153UDP-alpha-D-glucoseCombined sources1 Publication1
Metal bindingi164ZincCombined sources2 Publications1
<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 sitei166Tele-UMP-histidine intermediatePROSITE-ProRule annotation2 Publications1
Binding sitei168UDP-alpha-D-glucoseCombined sources1 Publication1
Metal bindingi182IronCombined sources2 Publications1
Metal bindingi281IronCombined sources2 Publications1
Metal bindingi296IronCombined sources2 Publications1
Metal bindingi298IronCombined sources2 Publications1
Binding sitei323UDP-alpha-D-glucoseCombined sources1 Publication1

<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 functionNucleotidyltransferase, Transferase
Biological processCarbohydrate metabolism, Galactose metabolism
LigandIron, Metal-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

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

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		2.7.7.12, 2026

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P09148

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

More...UniPathwayi		UPA00214

<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:
Galactose-1-phosphate uridylyltransferase (EC:2.7.7.123 Publications)
Short name:
Gal-1-P uridylyltransferase
Alternative name(s):
UDP-glucose--hexose-1-phosphate uridylyltransferase
<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:galT
Synonyms:galB
Ordered Locus Names:b0758, JW0741
<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>Mutagenesisi52C → S: Decreases enzyme activity 3000-fold. 1 Publication1
Mutagenesisi55C → S: Decreases enzyme activity 600-fold. 1 Publication1
Mutagenesisi115H → N: Decreases enzyme activity by 98%. 1 Publication1
Mutagenesisi160C → S or A: Slight inhibition of enzymatic activity. 1 Publication1
Mutagenesisi161S → A: 7000-fold reduction in specific activity. 1 Publication1
Mutagenesisi164H → N: Decreases enzyme activity 10000-fold. 1 Publication1
Mutagenesisi166H → G: Abolishes enzymatic activity. 1 Publication1
Mutagenesisi182E → A: Decreases enzyme activity by about 50%. Abolishes iron binding, but has no effect on zinc binding. 1 Publication1

Chemistry databases

Drug and drug target database

More...DrugBanki		DB01861, Uridine diphosphate glucose
DB03685, Uridine monophosphate
DB03435, Uridine-5'-Diphosphate

<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_00001698941 – 348Galactose-1-phosphate uridylyltransferaseAdd BLAST348

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P09148

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

More...PaxDbi		P09148

PRoteomics IDEntifications database

More...PRIDEi		P09148

<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

Homodimer.

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		4261703, 397 interactors

Database of interacting proteins

More...DIPi		DIP-9735N

Protein interaction database and analysis system

More...IntActi		P09148, 1 interactor

STRING: functional protein association networks

More...STRINGi		511145.b0758

<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

1348
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		P09148

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		P09148

<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>Regioni28 – 31UDP-alpha-D-glucose binding; shared with dimeric partnerCombined sources1 Publication4
Regioni77 – 78UDP-alpha-D-glucose bindingCombined sources1 Publication2
Regioni159 – 161UDP-alpha-D-glucose bindingCombined sources1 Publication3
Regioni311 – 312UDP-alpha-D-glucose binding; shared with dimeric partnerCombined sources1 Publication2
Regioni316 – 317UDP-alpha-D-glucose binding; shared with dimeric partnerCombined sources1 Publication2

<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 galactose-1-phosphate uridylyltransferase type 1 family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		COG1085, Bacteria

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_029960_0_0_6

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P09148

Database for complete collections of gene phylogenies

More...PhylomeDBi		P09148

Family and domain databases

Conserved Domains Database

More...CDDi		cd00608, GalT, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.428.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001937, GalP_UDPtransf1
IPR019779, GalP_UDPtransf1_His-AS
IPR005850, GalP_Utransf_C
IPR005849, GalP_Utransf_N
IPR036265, HIT-like_sf

The PANTHER Classification System

More...PANTHERi		PTHR11943, PTHR11943, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF02744, GalP_UDP_tr_C, 1 hit
PF01087, GalP_UDP_transf, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000808, GalT, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF54197, SSF54197, 2 hits

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00209, galT_1, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00117, GAL_P_UDP_TRANSF_I, 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.

P09148-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTQFNPVDHP HRRYNPLTGQ WILVSPHRAK RPWQGAQETP AKQVLPAHDP 
        60         70         80         90        100
DCFLCAGNVR VTGDKNPDYT GTYVFTNDFA ALMSDTPDAP ESHDPLMRCQ 
       110        120        130        140        150
SARGTSRVIC FSPDHSKTLP ELSVAALTEI VKTWQEQTAE LGKTYPWVQV 
       160        170        180        190        200
FENKGAAMGC SNPHPHGQIW ANSFLPNEAE REDRLQKEYF AEQKSPMLVD 
       210        220        230        240        250
YVQRELADGS RTVVETEHWL AVVPYWAAWP FETLLLPKAH VLRITDLTDA 
       260        270        280        290        300
QRSDLALALK KLTSRYDNLF QCSFPYSMGW HGAPFNGEEN QHWQLHAHFY 
       310        320        330        340 
PPLLRSATVR KFMVGYEMLA ETQRDLTAEQ AAERLRAVSD IHFRESGV
Length:348
Mass (Da):39,646
Last modified:November 1, 1997 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i3D55D2CB38D8C9A2
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 conflicti29 – 31AKR → LS in CAA29574 (PubMed:3022232).Curated3

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
X06226 Genomic DNA Translation: CAA29574.1
U00096 Genomic DNA Translation: AAC73845.1
AP009048 Genomic DNA Translation: BAA35420.1
X02306 Genomic DNA Translation: CAA26171.1

Protein sequence database of the Protein Information Resource

More...PIRi		S00722, XNECUD

NCBI Reference Sequences

More...RefSeqi		NP_415279.1, NC_000913.3
WP_000191497.1, NZ_SSZK01000002.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...EnsemblBacteriai		AAC73845; AAC73845; b0758
BAA35420; BAA35420; BAA35420

Database of genes from NCBI RefSeq genomes

More...GeneIDi		945357

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ecj:JW0741
eco:b0758

Pathosystems Resource Integration Center (PATRIC)

More...PATRICi		fig|1411691.4.peg.1520

<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
X06226 Genomic DNA Translation: CAA29574.1
U00096 Genomic DNA Translation: AAC73845.1
AP009048 Genomic DNA Translation: BAA35420.1
X02306 Genomic DNA Translation: CAA26171.1
PIRiS00722, XNECUD
RefSeqiNP_415279.1, NC_000913.3
WP_000191497.1, NZ_SSZK01000002.1

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
1GUPX-ray1.80A/B/C/D1-348[»]
1GUQX-ray1.80A/B/C/D1-348[»]
1HXPX-ray1.80A/B1-348[»]
1HXQX-ray1.86A/B1-348[»]
SMRiP09148
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi4261703, 397 interactors
DIPiDIP-9735N
IntActiP09148, 1 interactor
STRINGi511145.b0758

Chemistry databases

DrugBankiDB01861, Uridine diphosphate glucose
DB03685, Uridine monophosphate
DB03435, Uridine-5'-Diphosphate

Proteomic databases

jPOSTiP09148
PaxDbiP09148
PRIDEiP09148

Genome annotation databases

EnsemblBacteriaiAAC73845; AAC73845; b0758
BAA35420; BAA35420; BAA35420
GeneIDi945357
KEGGiecj:JW0741
eco:b0758
PATRICifig|1411691.4.peg.1520

Organism-specific databases

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

More...EchoBASEi		EB0361

Phylogenomic databases

eggNOGiCOG1085, Bacteria
HOGENOMiCLU_029960_0_0_6
InParanoidiP09148
PhylomeDBiP09148

Enzyme and pathway databases

UniPathwayiUPA00214
BioCyciEcoCyc:GALACTURIDYLYLTRANS-MONOMER
MetaCyc:GALACTURIDYLYLTRANS-MONOMER
BRENDAi2.7.7.12, 2026
SABIO-RKiP09148

Miscellaneous databases

EvolutionaryTraceiP09148

Protein Ontology

More...PROi		PR:P09148

Family and domain databases

CDDicd00608, GalT, 1 hit
Gene3Di3.30.428.10, 2 hits
InterProiView protein in InterPro
IPR001937, GalP_UDPtransf1
IPR019779, GalP_UDPtransf1_His-AS
IPR005850, GalP_Utransf_C
IPR005849, GalP_Utransf_N
IPR036265, HIT-like_sf
PANTHERiPTHR11943, PTHR11943, 1 hit
PfamiView protein in Pfam
PF02744, GalP_UDP_tr_C, 1 hit
PF01087, GalP_UDP_transf, 1 hit
PIRSFiPIRSF000808, GalT, 1 hit
SUPFAMiSSF54197, SSF54197, 2 hits
TIGRFAMsiTIGR00209, galT_1, 1 hit
PROSITEiView protein in PROSITE
PS00117, GAL_P_UDP_TRANSF_I, 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 nameiGAL7_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: P09148
Secondary accession number(s): P78270
<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: July 1, 1989
Last sequence update: November 1, 1997
Last modified: April 7, 2021
This is version 180 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, 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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