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Protein

4-aminobutyrate aminotransferase GabT

Gene

gabT

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 5'-phosphate1 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
Complete GO annotation...

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.
BRENDAi2.6.1.19. 2026.
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 Componenti: Chromosome UP000000625 Componenti: 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 – 1411Combined sources
Beta strandi22 – 3211Combined sources
Beta strandi34 – 374Combined sources
Beta strandi42 – 476Combined sources
Helixi48 – 514Combined sources
Helixi60 – 6910Combined sources
Turni70 – 723Combined sources
Turni78 – 803Combined sources
Helixi84 – 9613Combined sources
Beta strandi103 – 1108Combined sources
Helixi111 – 12616Combined sources
Beta strandi130 – 1345Combined sources
Helixi143 – 1486Combined sources
Turni153 – 1586Combined sources
Beta strandi164 – 1696Combined sources
Helixi174 – 1763Combined sources
Helixi180 – 19314Combined sources
Helixi197 – 1993Combined sources
Beta strandi200 – 2056Combined sources
Turni210 – 2134Combined sources
Helixi219 – 23214Combined sources
Beta strandi235 – 2395Combined sources
Turni241 – 2488Combined sources
Beta strandi249 – 2524Combined sources
Helixi253 – 2564Combined sources
Beta strandi262 – 2665Combined sources
Helixi268 – 2714Combined sources
Beta strandi273 – 2753Combined sources
Beta strandi277 – 2826Combined sources
Helixi283 – 2864Combined sources
Beta strandi297 – 3004Combined sources
Helixi302 – 31716Combined sources
Helixi320 – 34021Combined sources
Beta strandi345 – 3517Combined sources
Beta strandi354 – 3607Combined sources
Helixi361 – 3633Combined sources
Helixi370 – 38213Combined sources
Beta strandi388 – 3914Combined sources
Beta strandi396 – 3994Combined sources
Helixi407 – 42418Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP22256.
KOiK07250.
OMAiCGKAEIM.
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]
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

        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:July 31, 1991 - v1
Checksum:i02FC80FF0EAA1361
GO

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.
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:
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.
YP_490877.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

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

Proteomic databases

PaxDbiP22256.
PRIDEiP22256.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASEiEB0356.
EcoGeneiEG10361. gabT.

Phylogenomic databases

eggNOGiCOG0160.
HOGENOMiHOG000020206.
InParanoidiP22256.
KOiK07250.
OMAiCGKAEIM.
OrthoDBiEOG6QVRHN.
PhylomeDBiP22256.

Enzyme and pathway databases

UniPathwayiUPA00733.
BioCyciEcoCyc:GABATRANSAM-MONOMER.
ECOL316407:JW2637-MONOMER.
MetaCyc:GABATRANSAM-MONOMER.
RETL1328306-WGS:GSTH-5704-MONOMER.
RETL1328306-WGS:GSTH-96-MONOMER.
BRENDAi2.6.1.19. 2026.
SABIO-RKP22256.

Miscellaneous databases

EvolutionaryTraceiP22256.
PROiP22256.

Gene expression databases

GenevestigatoriP22256.

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]
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR00700. GABAtrnsam. 1 hit.
PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1989) [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(1996) [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(2005) [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(1989) [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(2001) [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(2003) [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(2009) [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(2003) [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(2004) [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: July 31, 1991
Last sequence update: July 31, 1991
Last modified: March 31, 2015
This is version 140 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.