Reviewed, UniProtKB/Swiss-Prot P40829 (GABT_MYCLE)

Names and origin

Protein names

Recommended name:
    4-aminobutyrate aminotransferase
    EC=2.6.1.19
Alternative name(s):
    Gamma-amino-N-butyrate transaminase
      Short name=GABA transaminase
    GABA aminotransferase
      Short name=GABA-AT
    L-AIBAT
    (S)-3-amino-2-methylpropionate transaminase
    EC=2.6.1.22
    Glutamate:succinic semialdehyde transaminase

Gene names

Name:	gabT
Ordered Locus Names:	ML0485
ORF Names:	MLCB1259.03c, B1177_F2_67

Organism

Mycobacterium leprae [Complete proteome] [HAMAP]

Taxonomic identifier

1769 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	446 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

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.
Pathway	Amino-acid degradation; 4-aminobutanoate degradation.
Sequence similarities	Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family.

Ontologies

Keywords
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	gamma-aminobutyric acid metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	(S)-3-amino-2-methylpropionate transaminase activity Inferred from electronic annotation. Source: EC 4-aminobutyrate transaminase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 446	446	4-aminobutyrate aminotransferase		PRO_0000120385
Amino acid modifications
	Modified residue	291	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P40829-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 576A6872DF6BDDC2	FASTA	446	47,215
	10 20 30 40 50 60 MTSVEQSRQL VTEIPGPVSL ELAKRLNAAV PRGVGVTLPV FVTRAAGGVI EDVDGNRLID 70 80 90 100 110 120 LGSGIAVTTI GNSSPRVVDA VRAQVADFTH TCFIITPYEE YVAVTEQLNR ITPGSGEKRS 130 140 150 160 170 180 VLFNSGAEAV ENSIKVARSY TRKPAVVAFD HAYHGRTNLT MALTAKSMPY KSGFGPFAPE 190 200 210 220 230 240 IYRAPLSYPY RDGLLNKDLA TDGKLAGARA INVIEKQVGA DDLAAVIIEP IQGEGGFIVP 250 260 270 280 290 300 AEGFLATLLD WCRKNNVMFI ADEVQTGFAR TGAMFACEHD GIVPDLICTA KGIADGLPLA 310 320 330 340 350 360 AVTGRAEIMN APHVSGLGGT FGGNPVACAA ALATITTIEN DGLIQRAQQI ERLITDRLLR 370 380 390 400 410 420 LQDADDRIGD VRGRGAMIAV ELVKSGTAEP DPELTEKVAT AAHATGVIIL TCGMFGNIIR 430 440 LLPPLTISDE LLAEGLDILS RILGDF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Smith D.R., Robison K. Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Massive gene decay in the leprosy bacillus." Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E., Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K., Duthoy S. , Feltwell T., Fraser A., Hamlin N., Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., Barrell B.G. Nature 409:1007-1011(2001) [PubMed: 11234002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TN.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00011 Genomic DNA. Translation: AAA17107.1. AL023591 Genomic DNA. Translation: CAA19078.1. AL583918 Genomic DNA. Translation: CAC29993.1.
PIR	S72743.
RefSeq	NP_301425.1.
3D structure databases
SMR	P40829. Positions 19-445.
ModBase	Search...
Genome annotation databases
GeneID	909237.
KEGG	mle:ML0485.
NMPDR	fig|272631.1.peg.297.
Organism-specific databases
Leproma	ML0485.
CMR	Search...
Phylogenomic databases
HOGENOM	HBG725944.
OMA	TTIGNSA.
Enzyme and pathway databases
BioCyc	MLEP272631:ML0485-MONOMER.
BRENDA	2.6.1.19. 808. 2.6.1.22. 808.
Family and domain databases
InterPro	IPR004632. 4NH2But_aminotransferase_bac. IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
PANTHER	PTHR11986. Aminotrans_3. 1 hit.
Pfam	PF00202. Aminotran_3. 1 hit. [Graphical view]
TIGRFAMs	TIGR00700. GABAtrnsam. 1 hit.
PROSITE	PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GABT_MYCLE

Accession

Primary (citable) accession number: P40829

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	February 9, 2010
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)