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P22256

- GABT_ECOLI

UniProt

P22256 - GABT_ECOLI

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Protein

4-aminobutyrate aminotransferase GabT

Gene
gabT, b2662, JW2637
Organism
Escherichia coli (strain K12)
Status
Reviewed - 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 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
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.
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.

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

« 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(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: July 9, 2014
This is version 133 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

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