4-aminobutyrate aminotransferase GabT
Details
- Name
- 4-aminobutyrate aminotransferase GabT
- Kind
- protein
- Synonyms
- (S)-3-amino-2-methylpropionate transaminase
- 2.6.1.19
- GABA aminotransferase
- GABA transaminase
- GABA-AT
- Gamma-amino-N-butyrate transaminase
- Glutamate:succinic semialdehyde transaminase
- L-AIBAT
- Gene Name
- gabT
- UniProtKB Entry
- P22256Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- Amino acid sequence
>lcl|BSEQ0011066|4-aminobutyrate aminotransferase GabT MNSNKELMQRRSQAIPRGVGQIHPIFADRAENCRVWDVEGREYLDFAGGIAVLNTGHLHP KVVAAVEAQLKKLSHTCFQVLAYEPYLELCEIMNQKVPGDFAKKTLLVTTGSEAVENAVK IARAATKRSGTIAFSGAYHGRTHYTLALTGKVNPYSAGMGLMPGHVYRALYPCPLHGISE DDAIASIHRIFKNDAAPEDIAAIVIEPVQGEGGFYASSPAFMQRLRALCDEHGIMLIADE VQSGAGRTGTLFAMEQMGVAPDLTTFAKSIAGGFPLAGVTGRAEVMDAVAPGGLGGTYAG NPIACVAALEVLKVFEQENLLQKANDLGQKLKDGLLAIAEKHPEIGDVRGLGAMIAIELF EDGDHNKPDAKLTAEIVARARDKGLILLSCGPYYNVLRILVPLTIEDAQIRQGLEIISQC FDEAKQ
- Number of residues
- 426
- Molecular Weight
- 45774.205
- Theoretical pI
- 6.1
- GO Classification
- Functions(S)-3-amino-2-methylpropionate transaminase activity / 4-aminobutyrate transaminase activity / identical protein binding / N2-acetyl-L-ornithine / pyridoxal phosphate bindingProcessesarginine biosynthetic process via ornithine / gamma-aminobutyric acid catabolic processComponentscytosol
- General Function
- Pyridoxal phosphate-dependent enzyme that catalyzes transamination between primary amines and alpha-keto acids. Catalyzes the transfer of the amino group from gamma-aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA) and glutamate (PubMed:15723541, PubMed:30498244). Thereby functions in a GABA degradation pathway that allows some E.coli strains to utilize GABA as a nitrogen source for growth (PubMed:12446648). Also catalyzes the conversion of 5-aminovalerate to glutarate semialdehyde, as part of a L-lysine degradation pathway that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate (PubMed:30498244).
- Specific Function
- 4-aminobutyrate transaminase activity
- Pfam Domain Function
- Aminotran_3 (PF00202)
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0011067|4-aminobutyrate aminotransferase GabT (gabT) ATGAACAGCAATAAAGAGTTAATGCAGCGCCGCAGTCAGGCGATTCCCCGTGGCGTTGGG CAAATTCACCCGATTTTCGCTGACCGCGCGGAAAACTGCCGGGTGTGGGACGTTGAAGGC CGTGAGTATCTTGATTTCGCGGGCGGGATTGCGGTGCTCAATACCGGGCACCTGCATCCG AAGGTGGTGGCCGCGGTGGAAGCGCAGTTGAAAAAACTGTCGCACACCTGCTTCCAGGTG CTGGCTTACGAGCCGTATCTGGAGCTGTGCGAGATTATGAATCAGAAGGTGCCGGGCGAT TTCGCCAAGAAAACGCTGCTGGTTACGACCGGTTCCGAAGCGGTGGAAAACGCGGTAAAA ATCGCCCGCGCCGCCACCAAACGTAGCGGCACCATCGCTTTTAGCGGCGCGTATCACGGG CGCACGCATTACACGCTGGCGCTGACCGGCAAGGTGAATCCGTACTCTGCGGGCATGGGG CTGATGCCGGGTCATGTTTATCGCGCGCTTTATCCTTGCCCGCTGCACGGCATAAGCGAG GATGACGCTATCGCCAGCATCCACCGGATCTTCAAAAATGATGCCGCGCCGGAAGATATC GCCGCCATCGTGATTGAGCCGGTTCAGGGCGAAGGCGGTTTCTACGCCTCGTCGCCAGCC TTTATGCAGCGTTTACGCGCTCTGTGTGACGAGCACGGGATCATGCTGATTGCCGATGAA GTGCAGAGCGGCGCGGGGCGTACCGGCACGCTGTTTGCGATGGAGCAGATGGGCGTTGCG CCGGATCTTACCACCTTTGCGAAATCGATCGCGGGCGGCTTCCCGCTGGCGGGCGTCACC GGGCGCGCGGAAGTAATGGATGCCGTCGCTCCAGGCGGTCTGGGCGGCACCTATGCGGGT AACCCGATTGCCTGCGTGGCTGCGCTGGAAGTGTTGAAGGTGTTTGAGCAGGAAAATCTG CTGCAAAAAGCCAACGATCTGGGGCAGAAGTTGAAAGACGGATTGCTGGCGATAGCCGAA AAACACCCGGAGATCGGCGACGTACGCGGGCTGGGGGCGATGATCGCCATTGAGCTGTTT GAAGACGGCGATCACAACAAGCCGGACGCCAAACTCACCGCCGAGATCGTGGCTCGCGCC CGCGATAAAGGCCTGATTCTTCTCTCCTGCGGCCCGTATTACAACGTGCTGCGCATCCTT GTACCGCTCACCATTGAAGACGCTCAGATCCGTCAGGGTCTGGAGATCATCAGCCAGTGT TTTGATGAGGCGAAGCAGTAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P22256 UniProtKB Entry Name GABT_ECOLI GenBank Protein ID 147902 GenBank Gene ID M88334 PDB ID(s) 1SF2, 1SFF, 1SZK, 1SZS, 1SZU KEGG ID ecj:JW2637 NCBI Gene ID 948067 - General References
- Bartsch K, von Johnn-Marteville A, Schulz A: 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). J Bacteriol. 1990 Dec;172(12):7035-42. [Article]
- 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, Horiuchi T, et al.: 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. DNA Res. 1997 Apr 28;4(2):91-113. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Schulz A, Taggeselle P, Tripier D, Bartsch K: Stereospecific production of the herbicide phosphinothricin (glufosinate) by transamination: isolation and characterization of a phosphinothricin-specific transaminase from Escherichia coli. Appl Environ Microbiol. 1990 Jan;56(1):1-6. [Article]
- Schneider BL, Ruback S, Kiupakis AK, Kasbarian H, Pybus C, Reitzer L: The Escherichia coli gabDTPC operon: specific gamma-aminobutyrate catabolism and nonspecific induction. J Bacteriol. 2002 Dec;184(24):6976-86. [Article]
- Metzner M, Germer J, Hengge R: Multiple stress signal integration in the regulation of the complex sigma S-dependent csiD-ygaF-gabDTP operon in Escherichia coli. Mol Microbiol. 2004 Feb;51(3):799-811. [Article]
- Kurihara S, Kato K, Asada K, Kumagai H, Suzuki H: A putrescine-inducible pathway comprising PuuE-YneI in which gamma-aminobutyrate is degraded into succinate in Escherichia coli K-12. J Bacteriol. 2010 Sep;192(18):4582-91. doi: 10.1128/JB.00308-10. Epub 2010 Jul 16. [Article]
- Liu W, Peterson PE, Carter RJ, Zhou X, Langston JA, Fisher AJ, Toney MD: Crystal structures of unbound and aminooxyacetate-bound Escherichia coli gamma-aminobutyrate aminotransferase. Biochemistry. 2004 Aug 31;43(34):10896-905. [Article]
- Liu W, Peterson PE, Langston JA, Jin X, Zhou X, Fisher AJ, Toney MD: Kinetic and crystallographic analysis of active site mutants of Escherichia coli gamma-aminobutyrate aminotransferase. Biochemistry. 2005 Mar 1;44(8):2982-92. [Article]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details Pyridoxamine-5'-Phosphate experimental unknown target Details 4'-Deoxy-4'-Acetylyamino-Pyridoxal-5'-Phosphate experimental unknown target Details