GABT_MYCLE
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 25-MAY-2022, entry version 132.
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; ORFNames=B1177_F2_67, MLCB1259.03c;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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.ML0485; -.
DR EnsemblBacteria; CAC29993; CAC29993; CAC29993.
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 OMA; GMTTQIY; -.
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; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00700; GABAtrnsam; 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
