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P22256

- GABT_ECOLI

UniProt

P22256 - GABT_ECOLI

Protein

4-aminobutyrate aminotransferase GabT

Gene

gabT

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Aug 1991)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of the amino group from gamma-aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA).1 Publication

    Catalytic activityi

    4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.
    (S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate.

    Cofactori

    Pyridoxal phosphate.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei138 – 1381Pyridoxal phosphate
    Binding sitei297 – 2971Pyridoxal phosphate

    GO - Molecular functioni

    1. (S)-3-amino-2-methylpropionate transaminase activity Source: UniProtKB-EC
    2. 4-aminobutyrate transaminase activity Source: EcoCyc
    3. pyridoxal phosphate binding Source: EcoCyc

    GO - Biological processi

    1. gamma-aminobutyric acid catabolic process Source: EcoCyc

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:GABATRANSAM-MONOMER.
    ECOL316407:JW2637-MONOMER.
    MetaCyc:GABATRANSAM-MONOMER.
    RETL1328306-WGS:GSTH-5704-MONOMER.
    RETL1328306-WGS:GSTH-96-MONOMER.
    SABIO-RKP22256.
    UniPathwayiUPA00733.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-aminobutyrate aminotransferase GabT (EC:2.6.1.19)
    Alternative name(s):
    (S)-3-amino-2-methylpropionate transaminase (EC:2.6.1.22)
    GABA aminotransferase
    Short name:
    GABA-AT
    Gamma-amino-N-butyrate transaminase
    Short name:
    GABA transaminase
    Glutamate:succinic semialdehyde transaminase
    L-AIBAT
    Gene namesi
    Name:gabT
    Ordered Locus Names:b2662, JW2637
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10361. gabT.

    Pathology & Biotechi

    Disruption phenotypei

    Cells show only 68% of the wild-type activity and are not able to utilize GABA as a nitrogen source.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4264264-aminobutyrate aminotransferase GabTPRO_0000120384Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei268 – 2681N6-(pyridoxal phosphate)lysine

    Proteomic databases

    PaxDbiP22256.
    PRIDEiP22256.

    Expressioni

    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).1 Publication

    Gene expression databases

    GenevestigatoriP22256.

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    DIPiDIP-9725N.
    IntActiP22256. 12 interactions.
    MINTiMINT-1274800.
    STRINGi511145.b2662.

    Structurei

    Secondary structure

    1
    426
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 1411
    Beta strandi22 – 3211
    Beta strandi34 – 374
    Beta strandi42 – 476
    Helixi48 – 514
    Helixi60 – 6910
    Turni70 – 723
    Turni78 – 803
    Helixi84 – 9613
    Beta strandi103 – 1108
    Helixi111 – 12616
    Beta strandi130 – 1345
    Helixi143 – 1486
    Turni153 – 1586
    Beta strandi164 – 1696
    Helixi174 – 1763
    Helixi180 – 19314
    Helixi197 – 1993
    Beta strandi200 – 2056
    Turni210 – 2134
    Helixi219 – 23214
    Beta strandi235 – 2395
    Turni241 – 2488
    Beta strandi249 – 2524
    Helixi253 – 2564
    Beta strandi262 – 2665
    Helixi268 – 2714
    Beta strandi273 – 2753
    Beta strandi277 – 2826
    Helixi283 – 2864
    Beta strandi297 – 3004
    Helixi302 – 31716
    Helixi320 – 34021
    Beta strandi345 – 3517
    Beta strandi354 – 3607
    Helixi361 – 3633
    Helixi370 – 38213
    Beta strandi388 – 3914
    Beta strandi396 – 3994
    Helixi407 – 42418

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP22256.
    SMRiP22256. Positions 2-426.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22256.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni111 – 1122Pyridoxal phosphate binding
    Regioni239 – 2424Pyridoxal phosphate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0160.
    HOGENOMiHOG000020206.
    KOiK07250.
    OMAiLDRCKAV.
    OrthoDBiEOG6QVRHN.
    PhylomeDBiP22256.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR004632. 4NH2But_aminotransferase_bac.
    IPR005814. Aminotrans_3.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PANTHERiPTHR11986. PTHR11986. 1 hit.
    PfamiPF00202. Aminotran_3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR00700. GABAtrnsam. 1 hit.
    PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P22256-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNSNKELMQR RSQAIPRGVG QIHPIFADRA ENCRVWDVEG REYLDFAGGI    50
    AVLNTGHLHP KVVAAVEAQL KKLSHTCFQV LAYEPYLELC EIMNQKVPGD 100
    FAKKTLLVTT GSEAVENAVK IARAATKRSG TIAFSGAYHG RTHYTLALTG 150
    KVNPYSAGMG LMPGHVYRAL YPCPLHGISE DDAIASIHRI FKNDAAPEDI 200
    AAIVIEPVQG EGGFYASSPA FMQRLRALCD EHGIMLIADE VQSGAGRTGT 250
    LFAMEQMGVA PDLTTFAKSI AGGFPLAGVT GRAEVMDAVA PGGLGGTYAG 300
    NPIACVAALE VLKVFEQENL LQKANDLGQK LKDGLLAIAE KHPEIGDVRG 350
    LGAMIAIELF EDGDHNKPDA KLTAEIVARA RDKGLILLSC GPYYNVLRIL 400
    VPLTIEDAQI RQGLEIISQC FDEAKQ 426
    Length:426
    Mass (Da):45,775
    Last modified:August 1, 1991 - v1
    Checksum:i02FC80FF0EAA1361
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    YP_490877.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75709; AAC75709; b2662.
    BAA16525; BAA16525; BAA16525.
    GeneIDi12930216.
    948067.
    KEGGiecj:Y75_p2605.
    eco:b2662.
    PATRICi32120714. VBIEscCol129921_2754.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M88334 Genomic DNA. Translation: AAC36832.1 .
    U00096 Genomic DNA. Translation: AAC75709.1 .
    AP009048 Genomic DNA. Translation: BAA16525.1 .
    PIRi A37846.
    RefSeqi NP_417148.1. NC_000913.3.
    YP_490877.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1SF2 X-ray 2.40 A/B/C/D 1-426 [» ]
    1SFF X-ray 1.90 A/B/C/D 1-426 [» ]
    1SZK X-ray 2.52 A/B/C/D 1-426 [» ]
    1SZS X-ray 2.10 A/B/C/D 1-426 [» ]
    1SZU X-ray 2.52 A/B/C/D 1-426 [» ]
    ProteinModelPortali P22256.
    SMRi P22256. Positions 2-426.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-9725N.
    IntActi P22256. 12 interactions.
    MINTi MINT-1274800.
    STRINGi 511145.b2662.

    Proteomic databases

    PaxDbi P22256.
    PRIDEi P22256.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75709 ; AAC75709 ; b2662 .
    BAA16525 ; BAA16525 ; BAA16525 .
    GeneIDi 12930216.
    948067.
    KEGGi ecj:Y75_p2605.
    eco:b2662.
    PATRICi 32120714. VBIEscCol129921_2754.

    Organism-specific databases

    EchoBASEi EB0356.
    EcoGenei EG10361. gabT.

    Phylogenomic databases

    eggNOGi COG0160.
    HOGENOMi HOG000020206.
    KOi K07250.
    OMAi LDRCKAV.
    OrthoDBi EOG6QVRHN.
    PhylomeDBi P22256.

    Enzyme and pathway databases

    UniPathwayi UPA00733 .
    BioCyci EcoCyc:GABATRANSAM-MONOMER.
    ECOL316407:JW2637-MONOMER.
    MetaCyc:GABATRANSAM-MONOMER.
    RETL1328306-WGS:GSTH-5704-MONOMER.
    RETL1328306-WGS:GSTH-96-MONOMER.
    SABIO-RK P22256.

    Miscellaneous databases

    EvolutionaryTracei P22256.
    PROi P22256.

    Gene expression databases

    Genevestigatori P22256.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi IPR004632. 4NH2But_aminotransferase_bac.
    IPR005814. Aminotrans_3.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    PANTHERi PTHR11986. PTHR11986. 1 hit.
    Pfami PF00202. Aminotran_3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR00700. GABAtrnsam. 1 hit.
    PROSITEi PS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular analysis of two genes of the Escherichia coli gab cluster: nucleotide sequence of the glutamate:succinic semialdehyde transaminase gene (gabT) and characterization of the succinic semialdehyde dehydrogenase gene (gabD)."
      Bartsch K., von Johnn-Marteville A., Schulz A.
      J. Bacteriol. 172:7035-7042(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    5. "Stereospecific production of the herbicide phosphinothricin (glufosinate) by transamination: isolation and characterization of a phosphinothricin-specific transaminase from Escherichia coli."
      Schulz A., Taggeselle P., Tripier D., Bartsch K.
      Appl. Environ. Microbiol. 56:1-6(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-30.
      Strain: K12.
    6. "The Escherichia coli gabDTPC operon: specific gamma-aminobutyrate catabolism and nonspecific induction."
      Schneider B.L., Ruback S., Kiupakis A.K., Kasbarian H., Pybus C., Reitzer L.
      J. Bacteriol. 184:6976-6986(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE.
      Strain: K12.
    7. "Multiple stress signal integration in the regulation of the complex sigma S-dependent csiD-ygaF-gabDTP operon in Escherichia coli."
      Metzner M., Germer J., Hengge R.
      Mol. Microbiol. 51:799-811(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
      Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
    8. "A putrescine-inducible pathway comprising PuuE-YneI in which gamma-aminobutyrate is degraded into succinate in Escherichia coli K-12."
      Kurihara S., Kato K., Asada K., Kumagai H., Suzuki H.
      J. Bacteriol. 192:4582-4591(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS A GABA AMINOTRANSFERASE, DISRUPTION PHENOTYPE.
      Strain: K12.
    9. "Crystal structures of unbound and aminooxyacetate-bound Escherichia coli gamma-aminobutyrate aminotransferase."
      Liu W., Peterson P.E., Carter R.J., Zhou X., Langston J.A., Fisher A.J., Toney M.D.
      Biochemistry 43:10896-10905(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL 5'-PHOSPHATE ANALOGS AND SUBUNIT.
      Strain: K12.
    10. "Kinetic and crystallographic analysis of active site mutants of Escherichia coli gamma-aminobutyrate aminotransferase."
      Liu W., Peterson P.E., Langston J.A., Jin X., Zhou X., Fisher A.J., Toney M.D.
      Biochemistry 44:2982-2992(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL 5'-PHOSPHATE ANALOGS, COFACTOR, SUBUNIT.
      Strain: K12.

    Entry informationi

    Entry nameiGABT_ECOLI
    AccessioniPrimary (citable) accession number: P22256
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: August 1, 1991
    Last modified: October 1, 2014
    This is version 134 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3