P22256 (GABT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	gabT
Ordered Locus Names:	b2662, JW2637

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	426 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	gamma-aminobutyric acid catabolic process Inferred from mutant phenotype. Source: EcoCyc
Molecular function	(S)-3-amino-2-methylpropionate transaminase activity Inferred from electronic annotation. Source: EC 4-aminobutyrate transaminase activity Inferred from direct assay Ref.5. Source: EcoCyc pyridoxal phosphate binding Inferred from direct assay Ref.9. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 426

426

4-aminobutyrate aminotransferase GabT

PRO_0000120384

Regions

Region

111 – 112

2

Pyridoxal phosphate binding

Region

239 – 242

4

Pyridoxal phosphate binding

Sites

Binding site

138

1

Pyridoxal phosphate

Binding site

297

1

Pyridoxal phosphate

Amino acid modifications

Modified residue

268

1

N6-(pyridoxal phosphate)lysine

Secondary structure

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426

Helix Strand Turn

Details...

Helix

4 – 14

11

Beta strand

22 – 32

11

Beta strand

34 – 37

4

Beta strand

42 – 47

6

Helix

48 – 51

4

Helix

60 – 69

10

Turn

70 – 72

3

Turn

78 – 80

3

Helix

84 – 96

13

Beta strand

103 – 110

8

Helix

111 – 126

16

Beta strand

130 – 134

5

Helix

143 – 148

6

Turn

153 – 156

4

Beta strand

164 – 169

6

Helix

174 – 176

3

Helix

180 – 193

14

Helix

197 – 199

3

Beta strand

200 – 205

6

Turn

210 – 213

4

Helix

219 – 232

14

Beta strand

235 – 239

5

Turn

241 – 248

8

Beta strand

249 – 252

4

Helix

253 – 256

4

Beta strand

262 – 266

5

Helix

268 – 271

4

Beta strand

277 – 282

6

Helix

283 – 286

4

Beta strand

297 – 300

4

Helix

302 – 317

16

Helix

320 – 339

20

Beta strand

345 – 349

5

Beta strand

355 – 360

6

Helix

361 – 363

3

Helix

370 – 382

13

Beta strand

388 – 391

4

Beta strand

396 – 399

4

Helix

407 – 425

19

Sequences

	Sequence		Length	Mass (Da)
	P22256 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 02FC80FF0EAA1361	FASTA	426	45,775
	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

References

	« Hide 'large scale' referencesShow '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: 2254272] [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: 9205837] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 2178550] [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: 12446648] [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: 14731280] [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: 20639325] [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: 15323550] [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: 15723541] [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.

PIR

A37846.

RefSeq

NP_417148.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P22256.

SMR

P22256. Positions 2-426.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-9725N.

IntAct

P22256. 10 interactions.

MINT

MINT-1274800.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000003590; EBESCP00000003590; EBESCG00000002932.
EBESCT00000003591; EBESCP00000003591; EBESCG00000002932.
EBESCT00000003592; EBESCP00000003592; EBESCG00000002932.
EBESCT00000014957; EBESCP00000014248; EBESCG00000014017.

GeneID

948067.

GenomeReviews

Gene locus JW2637 in contig AP009048_GR.
Gene locus b2662 in contig U00096_GR.

KEGG

ecj:JW2637.
eco:b2662.

PATRIC

32120714. VBIEscCol129921_2754.

Organism-specific databases

EchoBASE

EB0356.

EcoGene

EG10361. gabT.

Phylogenomic databases

eggNOG

COG0160.

GeneTree

EBGT00050000010246.

HOGENOM

HBG725944.

OMA

LQACYEQ.

PhylomeDB

P22256.

ProtClustDB

PRK08088.

Enzyme and pathway databases

BioCyc

EcoCyc:GABATRANSAM-MONOMER.
MetaCyc:GABATRANSAM-MONOMER.

Gene expression databases

Genevestigator

P22256.

Family and domain databases

InterPro

IPR004632. 4NH2But_aminotransferase_bac.
IPR005814. Aminotrans_3.
IPR015424. PyrdxlP-dep_Trfase_major_dom.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.

KO

K07250.

PANTHER

PTHR11986. Aminotrans_3. 1 hit.

Pfam

PF00202. Aminotran_3. 1 hit.
[Graphical view]

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

TIGRFAMs

TIGR00700. GABAtrnsam. 1 hit.

PROSITE

PS00600. AA_TRANSFER_CLASS_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GABT_ECOLI

Accession

Primary (citable) accession number: P22256

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	January 25, 2012
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program