Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 167 (08 May 2019)
Sequence version 1 (01 Aug 1991)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

4-aminobutyrate aminotransferase GabT

Gene

gabT

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

Pyridoxal phosphate-dependent enzyme that catalyzes transamination between primary amines and alpha-keto acids. Catalyzes the transfer of the amino group from gamma-aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA) and glutamate (PubMed:15723541, PubMed:30498244). Thereby functions in a GABA degradation pathway that allows some E.coli strains to utilize GABA as a nitrogen source for growth (PubMed:12446648). Also catalyzes the conversion of 5-aminovalerate to glutarate semialdehyde, as part of a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate (PubMed:30498244).3 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

pyridoxal 5'-phosphate2 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

kcat is 47.4 sec(-1) with 4-aminobutanoate as substrate (at 25 degrees Celsius and pH 7.8).1 Publication
  1. KM=197 µM for 4-aminobutanoate (measured for a coupled GabT/GabD reaction)1 Publication
  2. KM=439 µM for 5-aminopentanoate (measured for a coupled GabT/GabD reaction)1 Publication
  3. KM=5.8 mM for 4-aminobutanoate (at 25 degrees Celsius and pH 7.8)1 Publication
  4. KM=1.07 mM for 2-oxoglutarate (at 25 degrees Celsius and pH 7.8)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: 4-aminobutanoate degradation

    This protein is involved in the pathway 4-aminobutanoate degradation, which is part of Amino-acid degradation.1 Publication
    View all proteins of this organism that are known to be involved in the pathway 4-aminobutanoate degradation and in Amino-acid degradation.

    Pathwayi: Amino-acid degradation

    This protein is involved in Amino-acid degradation.1 Publication
    View all proteins of this organism that are known to be involved in Amino-acid degradation.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei242Pyridoxal phosphate2 Publications1
    Binding sitei297Pyridoxal phosphate2 Publications1

    <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

    • arginine biosynthetic process via ornithine Source: EcoCyc
    • gamma-aminobutyric acid catabolic process Source: EcoCyc

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

    Molecular functionAminotransferase, Transferase
    LigandPyridoxal phosphate

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    EcoCyc:GABATRANSAM-MONOMER
    ECOL316407:JW2637-MONOMER
    MetaCyc:GABATRANSAM-MONOMER

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.6.1.19 2026

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P22256

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

    More...
    UniPathwayi
    UPA00733

    <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:
    4-aminobutyrate aminotransferase GabT (EC:2.6.1.192 Publications)
    Alternative name(s):
    5-aminovalerate transaminase1 Publication (EC:2.6.1.481 Publication)
    GABA aminotransferase
    Short name:
    GABA-AT
    Gamma-amino-N-butyrate transaminase
    Short name:
    GABA transaminase
    Glutamate:succinic semialdehyde transaminase
    L-AIBAT
    <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:gabT
    Ordered Locus Names:b2662, JW2637
    <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
    EG10361 gabT

    <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

    <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 are not able to utilize GABA as a nitrogen source, in contrast to wild-type, but grow normally with arginine, ornithine, putrescine and agmatine (PubMed:12446648). Cells show only 68% of the wild-type GABA aminotransferase activity (PubMed:20639325).2 Publications

    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>Mutagenesisi50I → Q: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA. 1 Publication1
    Mutagenesisi211E → S: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA. 1 Publication1
    Mutagenesisi241V → A: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA. 1 Publication1

    Chemistry databases

    Drug and drug target database

    More...
    DrugBanki
    DB02783 4'-Deoxy-4'-Acetylyamino-Pyridoxal-5'-Phosphate
    DB02142 Pyridoxamine-5'-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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001203841 – 4264-aminobutyrate aminotransferase GabTAdd BLAST426

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei268N6-(pyridoxal phosphate)lysineCombined sources2 Publications1

    Proteomic databases

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P22256

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P22256

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

    More...
    PaxDbi
    P22256

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P22256

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Induced by RpoS in response to multiple stress conditions, including shifts to acidic pH or high osmolarity as well as starvation or stationary phase. Catabolite repression by glucose (repression relieved by GABA) (PubMed:14731280). Makes part of the gabDTPC operon, which is up-regulated by nitrogen limitation (PubMed:12446648).2 Publications

    <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

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    4259210, 22 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-9725N

    Protein interaction database and analysis system

    More...
    IntActi
    P22256, 12 interactors

    STRING: functional protein association networks

    More...
    STRINGi
    511145.b2662

    <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

    1426
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    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
    1SF2X-ray2.40A/B/C/D1-426[»]
    1SFFX-ray1.90A/B/C/D1-426[»]
    1SZKX-ray2.52A/B/C/D1-426[»]
    1SZSX-ray2.10A/B/C/D1-426[»]
    1SZUX-ray2.52A/B/C/D1-426[»]

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

    More...
    SMRi
    P22256

    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
    P22256

    <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>Regioni111 – 112Pyridoxal phosphate binding2 Publications2

    <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
    ENOG4108JPW Bacteria
    COG0160 LUCA

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000020206

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P22256

    KEGG Orthology (KO)

    More...
    KOi
    K07250

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    P22256

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00610 OAT_like, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.640.10, 1 hit
    3.90.1150.10, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR004632 4NH2But_aminotransferase_bac
    IPR005814 Aminotrans_3
    IPR015424 PyrdxlP-dep_Trfase
    IPR015422 PyrdxlP-dep_Trfase_dom1
    IPR015421 PyrdxlP-dep_Trfase_major

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00202 Aminotran_3, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF000521 Transaminase_4ab_Lys_Orn, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF53383 SSF53383, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR00700 GABAtrnsam, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00600 AA_TRANSFER_CLASS_3, 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.

    P22256-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MNSNKELMQR RSQAIPRGVG QIHPIFADRA ENCRVWDVEG REYLDFAGGI
    60 70 80 90 100
    AVLNTGHLHP KVVAAVEAQL KKLSHTCFQV LAYEPYLELC EIMNQKVPGD
    110 120 130 140 150
    FAKKTLLVTT GSEAVENAVK IARAATKRSG TIAFSGAYHG RTHYTLALTG
    160 170 180 190 200
    KVNPYSAGMG LMPGHVYRAL YPCPLHGISE DDAIASIHRI FKNDAAPEDI
    210 220 230 240 250
    AAIVIEPVQG EGGFYASSPA FMQRLRALCD EHGIMLIADE VQSGAGRTGT
    260 270 280 290 300
    LFAMEQMGVA PDLTTFAKSI AGGFPLAGVT GRAEVMDAVA PGGLGGTYAG
    310 320 330 340 350
    NPIACVAALE VLKVFEQENL LQKANDLGQK LKDGLLAIAE KHPEIGDVRG
    360 370 380 390 400
    LGAMIAIELF EDGDHNKPDA KLTAEIVARA RDKGLILLSC GPYYNVLRIL
    410 420
    VPLTIEDAQI RQGLEIISQC FDEAKQ
    Length:426
    Mass (Da):45,775
    Last modified:August 1, 1991 - 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:i02FC80FF0EAA1361
    GO

    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
    M88334 Genomic DNA Translation: AAC36832.1
    U00096 Genomic DNA Translation: AAC75709.1
    AP009048 Genomic DNA Translation: BAA16525.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A37846

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_417148.1, NC_000913.3
    WP_001087611.1, NZ_LN832404.1

    Genome annotation databases

    Ensembl bacterial and archaeal genome annotation project

    More...
    EnsemblBacteriai
    AAC75709; AAC75709; b2662
    BAA16525; BAA16525; BAA16525

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    948067

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    ecj:JW2637
    eco:b2662

    Pathosystems Resource Integration Center (PATRIC)

    More...
    PATRICi
    fig|1411691.4.peg.4079

    <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
    M88334 Genomic DNA Translation: AAC36832.1
    U00096 Genomic DNA Translation: AAC75709.1
    AP009048 Genomic DNA Translation: BAA16525.1
    PIRiA37846
    RefSeqiNP_417148.1, NC_000913.3
    WP_001087611.1, NZ_LN832404.1

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1SF2X-ray2.40A/B/C/D1-426[»]
    1SFFX-ray1.90A/B/C/D1-426[»]
    1SZKX-ray2.52A/B/C/D1-426[»]
    1SZSX-ray2.10A/B/C/D1-426[»]
    1SZUX-ray2.52A/B/C/D1-426[»]
    SMRiP22256
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259210, 22 interactors
    DIPiDIP-9725N
    IntActiP22256, 12 interactors
    STRINGi511145.b2662

    Chemistry databases

    DrugBankiDB02783 4'-Deoxy-4'-Acetylyamino-Pyridoxal-5'-Phosphate
    DB02142 Pyridoxamine-5'-Phosphate

    Proteomic databases

    EPDiP22256
    jPOSTiP22256
    PaxDbiP22256
    PRIDEiP22256

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75709; AAC75709; b2662
    BAA16525; BAA16525; BAA16525
    GeneIDi948067
    KEGGiecj:JW2637
    eco:b2662
    PATRICifig|1411691.4.peg.4079

    Organism-specific databases

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

    More...
    EchoBASEi
    EB0356
    EcoGeneiEG10361 gabT

    Phylogenomic databases

    eggNOGiENOG4108JPW Bacteria
    COG0160 LUCA
    HOGENOMiHOG000020206
    InParanoidiP22256
    KOiK07250
    PhylomeDBiP22256

    Enzyme and pathway databases

    UniPathwayi
    UPA00733

    BioCyciEcoCyc:GABATRANSAM-MONOMER
    ECOL316407:JW2637-MONOMER
    MetaCyc:GABATRANSAM-MONOMER
    BRENDAi2.6.1.19 2026
    SABIO-RKiP22256

    Miscellaneous databases

    EvolutionaryTraceiP22256

    Protein Ontology

    More...
    PROi
    PR:P22256

    Family and domain databases

    CDDicd00610 OAT_like, 1 hit
    Gene3Di3.40.640.10, 1 hit
    3.90.1150.10, 1 hit
    InterProiView protein in InterPro
    IPR004632 4NH2But_aminotransferase_bac
    IPR005814 Aminotrans_3
    IPR015424 PyrdxlP-dep_Trfase
    IPR015422 PyrdxlP-dep_Trfase_dom1
    IPR015421 PyrdxlP-dep_Trfase_major
    PfamiView protein in Pfam
    PF00202 Aminotran_3, 1 hit
    PIRSFiPIRSF000521 Transaminase_4ab_Lys_Orn, 1 hit
    SUPFAMiSSF53383 SSF53383, 1 hit
    TIGRFAMsiTIGR00700 GABAtrnsam, 1 hit
    PROSITEiView protein in PROSITE
    PS00600 AA_TRANSFER_CLASS_3, 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 nameiGABT_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: P22256
    <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: August 1, 1991
    Last sequence update: August 1, 1991
    Last modified: May 8, 2019
    This is version 167 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, Direct protein sequencing, 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. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    4. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health

    We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

    Do not show this banner again