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P22256 (GABT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:gabT
Ordered Locus Names:b2662, JW2637
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length426 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of the amino group from gamma-aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA). Ref.8

Catalytic activity

4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.

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

Cofactor

Pyridoxal phosphate. Ref.10

Pathway

Amino-acid degradation; 4-aminobutanoate degradation.

Subunit structure

Homotetramer. Ref.9 Ref.10

Induction

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). Ref.7

Disruption phenotype

Cells show only 68% of the wild-type activity and are not able to utilize GABA as a nitrogen source. Ref.6 Ref.8

Sequence similarities

Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4264264-aminobutyrate aminotransferase GabT
PRO_0000120384

Regions

Region111 – 1122Pyridoxal phosphate binding
Region239 – 2424Pyridoxal phosphate binding

Sites

Binding site1381Pyridoxal phosphate
Binding site2971Pyridoxal phosphate

Amino acid modifications

Modified residue2681N6-(pyridoxal phosphate)lysine

Secondary structure

......................................................................... 426
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P22256 [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: 02FC80FF0EAA1361

FASTA42645,775
        10         20         30         40         50         60 
MNSNKELMQR RSQAIPRGVG QIHPIFADRA ENCRVWDVEG REYLDFAGGI AVLNTGHLHP 

        70         80         90        100        110        120 
KVVAAVEAQL KKLSHTCFQV LAYEPYLELC EIMNQKVPGD FAKKTLLVTT GSEAVENAVK 

       130        140        150        160        170        180 
IARAATKRSG TIAFSGAYHG RTHYTLALTG KVNPYSAGMG LMPGHVYRAL YPCPLHGISE 

       190        200        210        220        230        240 
DDAIASIHRI FKNDAAPEDI AAIVIEPVQG EGGFYASSPA FMQRLRALCD EHGIMLIADE 

       250        260        270        280        290        300 
VQSGAGRTGT LFAMEQMGVA PDLTTFAKSI AGGFPLAGVT GRAEVMDAVA PGGLGGTYAG 

       310        320        330        340        350        360 
NPIACVAALE VLKVFEQENL LQKANDLGQK LKDGLLAIAE KHPEIGDVRG LGAMIAIELF 

       370        380        390        400        410        420 
EDGDHNKPDA KLTAEIVARA RDKGLILLSC GPYYNVLRIL VPLTIEDAQI RQGLEIISQC 


FDEAKQ 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M88334 Genomic DNA. Translation: AAC36832.1.
U00096 Genomic DNA. Translation: AAC75709.1.
AP009048 Genomic DNA. Translation: BAA16525.1.
PIRA37846.
RefSeqNP_417148.1. NC_000913.3.
YP_490877.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalP22256.
SMRP22256. Positions 2-426.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9725N.
IntActP22256. 12 interactions.
MINTMINT-1274800.
STRING511145.b2662.

Proteomic databases

PaxDbP22256.
PRIDEP22256.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75709; AAC75709; b2662.
BAA16525; BAA16525; BAA16525.
GeneID12930216.
948067.
KEGGecj:Y75_p2605.
eco:b2662.
PATRIC32120714. VBIEscCol129921_2754.

Organism-specific databases

EchoBASEEB0356.
EcoGeneEG10361. gabT.

Phylogenomic databases

eggNOGCOG0160.
HOGENOMHOG000020206.
KOK07250.
OMALDRCKAV.
OrthoDBEOG6QVRHN.
PhylomeDBP22256.

Enzyme and pathway databases

BioCycEcoCyc:GABATRANSAM-MONOMER.
ECOL316407:JW2637-MONOMER.
MetaCyc:GABATRANSAM-MONOMER.
RETL1328306-WGS:GSTH-5704-MONOMER.
RETL1328306-WGS:GSTH-96-MONOMER.
SABIO-RKP22256.
UniPathwayUPA00733.

Gene expression databases

GenevestigatorP22256.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProIPR004632. 4NH2But_aminotransferase_bac.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PANTHERPTHR11986. PTHR11986. 1 hit.
PfamPF00202. Aminotran_3. 1 hit.
[Graphical view]
PIRSFPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR00700. GABAtrnsam. 1 hit.
PROSITEPS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP22256.
PROP22256.

Entry information

Entry nameGABT_ECOLI
AccessionPrimary (citable) accession number: P22256
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: July 9, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene