RegulonDB RegulonDB 11.1: Gene Form
   

gabT gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

gabD gabP gabT csiRp5 csiRp5 TSS_2986 TSS_2986 csiRp3 csiRp3

Gene      
Name: gabT    Texpresso search in the literature
Synonym(s): ECK2656, EG10361, b2662
Genome position(nucleotides): 2792735 --> 2794015
Strand: forward
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 59.33
External database links:  
ASAP:
 ABE-0008760
CGSC:
 727
ECHOBASE:
 EB0356
ECOLIHUB:
 gabT
OU-MICROARRAY:
 b2662
STRING:
 511145.b2662
COLOMBOS: gabT


Product      
Name: 4-aminobutyrate aminotransferase GabT
Synonym(s): GabT
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 45.775
Isoelectric point: 6.097
Motif(s):
 
Type Positions Sequence Comment
16 -> 420 PRGVGQIHPIFADRAENCRVWDVEGREYLDFAGGIAVLNTGHLHPKVVAAVEAQLKKLSHTCFQVLAYEPYLELCEIMNQKVPGDFAKKTLLVTTGSEAVENAVKIARAATKRSGTIAFSGAYHGRTHYTLALTGKVNPYSAGMGLMPGHVYRALYPCPLHGISEDDAIASIHRIFKNDAAPEDIAAIVIEPVQGEGGFYASSPAFMQRLRALCDEHGIMLIADEVQSGAGRTGTLFAMEQMGVAPDLTTFAKSIAGGFPLAGVTGRAEVMDAVAPGGLGGTYAGNPIACVAALEVLKVFEQENLLQKANDLGQKLKDGLLAIAEKHPEIGDVRGLGAMIAIELFEDGDHNKPDAKLTAEIVARARDKGLILLSCGPYYNVLRILVPLTIEDAQIRQGLEIISQC
50 -> 50 I UniProt: 3-fold decrease in catalytic activity and 12-fold decrease in affinity for GABA..
111 -> 112 GS UniProt: Pyridoxal phosphate binding; Sequence Annotation Type: region of interest.
211 -> 211 E UniProt: 100-fold decrease in catalytic activity and 15-fold decrease in affinity for GABA..
241 -> 241 V UniProt: 25-fold decrease in catalytic activity and 5-fold decrease in affinity for GABA..

 
Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.7 - central intermediary metabolism --> 1.7.31 - aminobutyrate catabolism
  1 - metabolism --> 1.7 - central intermediary metabolism --> 1.7.32 - putrescine catabolism
Gene Ontology Terms (GO)  
cellular_component GO:0005829 - cytosol
molecular_function GO:0034386 - 4-aminobutyrate:2-oxoglutarate transaminase activity
GO:0047589 - 5-aminovalerate transaminase activity
GO:0003824 - catalytic activity
GO:0016740 - transferase activity
GO:0008483 - transaminase activity
GO:0030170 - pyridoxal phosphate binding
GO:0003867 - 4-aminobutyrate transaminase activity
GO:0003992 - N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
GO:0042803 - protein homodimerization activity
biological_process GO:0009448 - gamma-aminobutyric acid metabolic process
GO:0009450 - gamma-aminobutyric acid catabolic process
GO:0042450 - arginine biosynthetic process via ornithine
Note(s): Note(s): ...[more].
Reference(s): [1] Chung DH., et al., 2017
[2] Kim SH., et al., 2010
[3] Pham VD., et al., 2016
[4] Schneider BL., et al., 2012
[5] Spiteri D., et al., 2017
External database links:  
ALPHAFOLD:
 P22256
DIP:
 DIP-9725N
ECOCYC:
 GABATRANSAM-MONOMER
ECOLIWIKI:
 b2662
INTERPRO:
 IPR015421
INTERPRO:
 IPR005814
INTERPRO:
 IPR004632
INTERPRO:
 IPR015424
INTERPRO:
 IPR015422
MODBASE:
 P22256
PDB:
 1SF2
PDB:
 1SZU
PDB:
 1SFF
PDB:
 1SZS
PDB:
 1SZK
PFAM:
 PF00202
PRIDE:
 P22256
PROSITE:
 PS00600
REFSEQ:
 NP_417148
SMR:
 P22256
UNIPROT:
 P22256


Operon      
Name: glaH-lhgD-gabDTP         
Operon arrangement:
Transcription unit        Promoter
csiD-ygaF-gabDTP
gabDTP
gabDTP
gabDTP


Transcriptional Regulation      
Display Regulation             
Activated by: Nac, CRP, H-NS, Lrp
Repressed by: GlaR


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter csiRp3 2795471 forward nd [COMP-AINF] [6]
  promoter TSS_2986 2795625 forward nd [RS-EPT-CBR] [7]
  promoter csiRp5 2795643 forward nd [COMP-AINF] [6]


Evidence    

 [COMP-AINF] Inferred computationally without human oversight

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates


Reference(s)    

 [1] Chung DH., Potter SC., Tanomrat AC., Ravikumar KM., Toney MD., 2017, Site-directed mutant libraries for isolating minimal mutations yielding functional changes., Protein Eng Des Sel 30(5):347-357

 [2] Kim SH., Schneider BL., Reitzer L., 2010, Genetics and regulation of the major enzymes of alanine synthesis in Escherichia coli., J Bacteriol 192(20):5304-11

 [3] Pham VD., Somasundaram S., Park SJ., Lee SH., Hong SH., 2016, Co-Localization of GABA Shunt Enzymes for the Efficient Production of Gamma-Aminobutyric Acid via GABA Shunt Pathway in Escherichia coli., J Microbiol Biotechnol 26(4):710-6

 [4] Schneider BL., Reitzer L., 2012, Pathway and enzyme redundancy in putrescine catabolism in Escherichia coli., J Bacteriol 194(15):4080-8

 [5] Spiteri D., Chot-Plassot C., Sclear J., Karatzas KA., Scerri C., Valdramidis VP., 2017, Ultrasound processing of liquid system(s) and its antimicrobial mechanism of action., Lett Appl Microbiol 65(4):313-318

 [6] Huerta AM., Collado-Vides J., 2003, Sigma70 promoters in Escherichia coli: specific transcription in dense regions of overlapping promoter-like signals., J Mol Biol 333(2):261-78

 [7] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.

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