ID   GABT_MYCLE              Reviewed;         446 AA.
AC   P40829;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=4-aminobutyrate aminotransferase;
DE            EC=2.6.1.19;
DE   AltName: Full=(S)-3-amino-2-methylpropionate transaminase;
DE            EC=2.6.1.22;
DE   AltName: Full=GABA aminotransferase;
DE            Short=GABA-AT;
DE   AltName: Full=Gamma-amino-N-butyrate transaminase;
DE            Short=GABA transaminase;
DE   AltName: Full=Glutamate:succinic semialdehyde transaminase;
DE   AltName: Full=L-AIBAT;
GN   Name=gabT; OrderedLocusNames=ML0485;
GN   ORFNames=B1177_F2_67, MLCB1259.03c;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + 4-aminobutanoate = L-glutamate + succinate
CC         semialdehyde; Xref=Rhea:RHEA:23352, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57706, ChEBI:CHEBI:59888; EC=2.6.1.19;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-
CC         oxopropanoate + L-glutamate; Xref=Rhea:RHEA:13993, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57700, ChEBI:CHEBI:58655; EC=2.6.1.22;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; U00011; AAA17107.1; -; Genomic_DNA.
DR   EMBL; AL023591; CAA19078.1; -; Genomic_DNA.
DR   EMBL; AL583918; CAC29993.1; -; Genomic_DNA.
DR   PIR; S72743; S72743.
DR   RefSeq; NP_301425.1; NC_002677.1.
DR   RefSeq; WP_010907749.1; NC_002677.1.
DR   AlphaFoldDB; P40829; -.
DR   SMR; P40829; -.
DR   STRING; 272631.gene:17574306; -.
DR   KEGG; mle:ML0485; -.
DR   PATRIC; fig|272631.5.peg.849; -.
DR   Leproma; ML0485; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_11; -.
DR   OrthoDB; 9801052at2; -.
DR   UniPathway; UPA00733; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR049704; Aminotrans_3_PPA_site.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR00700; GABAtrnsam; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..446
FT                   /note="4-aminobutyrate aminotransferase"
FT                   /id="PRO_0000120385"
FT   MOD_RES         291
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   446 AA;  47215 MW;  576A6872DF6BDDC2 CRC64;
     MTSVEQSRQL VTEIPGPVSL ELAKRLNAAV PRGVGVTLPV FVTRAAGGVI EDVDGNRLID
     LGSGIAVTTI GNSSPRVVDA VRAQVADFTH TCFIITPYEE YVAVTEQLNR ITPGSGEKRS
     VLFNSGAEAV ENSIKVARSY TRKPAVVAFD HAYHGRTNLT MALTAKSMPY KSGFGPFAPE
     IYRAPLSYPY RDGLLNKDLA TDGKLAGARA INVIEKQVGA DDLAAVIIEP IQGEGGFIVP
     AEGFLATLLD WCRKNNVMFI ADEVQTGFAR TGAMFACEHD GIVPDLICTA KGIADGLPLA
     AVTGRAEIMN APHVSGLGGT FGGNPVACAA ALATITTIEN DGLIQRAQQI ERLITDRLLR
     LQDADDRIGD VRGRGAMIAV ELVKSGTAEP DPELTEKVAT AAHATGVIIL TCGMFGNIIR
     LLPPLTISDE LLAEGLDILS RILGDF
//