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Protein

4-aminobutyrate aminotransferase GabT

Gene

gabT

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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: 4-aminobutanoate degradation

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei138Pyridoxal phosphate1
Binding sitei297Pyridoxal phosphate1

GO - Molecular functioni

GO - Biological processi

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

Keywordsi

Molecular functionAminotransferase, Transferase
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyciEcoCyc:GABATRANSAM-MONOMER
MetaCyc:GABATRANSAM-MONOMER
BRENDAi2.6.1.19 2026
SABIO-RKiP22256
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10361 gabT

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

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

Chemistry databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001203841 – 4264-aminobutyrate aminotransferase GabTAdd BLAST426

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei268N6-(pyridoxal phosphate)lysine1

Proteomic databases

EPDiP22256
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

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

BioGridi425921022 interactors.
DIPiDIP-9725N
IntActiP22256 12 interactors.
STRINGi316385.ECDH10B_2829

Structurei

Secondary structure

1426
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 14Combined sources11
Beta strandi22 – 32Combined sources11
Beta strandi34 – 37Combined sources4
Beta strandi42 – 47Combined sources6
Helixi48 – 51Combined sources4
Helixi60 – 69Combined sources10
Turni70 – 72Combined sources3
Turni78 – 80Combined sources3
Helixi84 – 96Combined sources13
Beta strandi103 – 110Combined sources8
Helixi111 – 126Combined sources16
Beta strandi130 – 134Combined sources5
Helixi143 – 148Combined sources6
Turni153 – 158Combined sources6
Beta strandi164 – 169Combined sources6
Helixi174 – 176Combined sources3
Helixi180 – 193Combined sources14
Helixi197 – 199Combined sources3
Beta strandi200 – 205Combined sources6
Turni210 – 213Combined sources4
Helixi219 – 232Combined sources14
Beta strandi235 – 239Combined sources5
Turni241 – 248Combined sources8
Beta strandi249 – 252Combined sources4
Helixi253 – 256Combined sources4
Beta strandi262 – 266Combined sources5
Helixi268 – 271Combined sources4
Beta strandi273 – 275Combined sources3
Beta strandi277 – 282Combined sources6
Helixi283 – 286Combined sources4
Beta strandi297 – 300Combined sources4
Helixi302 – 317Combined sources16
Helixi320 – 340Combined sources21
Beta strandi345 – 351Combined sources7
Beta strandi354 – 360Combined sources7
Helixi361 – 363Combined sources3
Helixi370 – 382Combined sources13
Beta strandi388 – 391Combined sources4
Beta strandi396 – 399Combined sources4
Helixi407 – 424Combined sources18

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[»]
ProteinModelPortaliP22256
SMRiP22256
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22256

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni111 – 112Pyridoxal phosphate binding2
Regioni239 – 242Pyridoxal phosphate binding4

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4108JPW Bacteria
COG0160 LUCA
HOGENOMiHOG000020206
InParanoidiP22256
KOiK07250
OMAiRVGNYLT
PhylomeDBiP22256

Family and domain databases

CDDicd00610 OAT_like, 1 hit
Gene3Di3.40.640.101 hit
3.90.1150.102 hits
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

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:August 1, 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
WP_001087611.1, NZ_LN832404.1

Genome annotation databases

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

Similar proteinsi

Entry informationi

Entry nameiGABT_ECOLI
AccessioniPrimary (citable) accession number: P22256
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: March 28, 2018
This is version 161 of the entry and version 1 of the sequence. See 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