ID   GABT_MYCTO              Reviewed;         449 AA.
AC   P9WQ78; L0TA45; P63504; Q50632;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 42.
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=MT2666;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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         Evidence={ECO:0000250};
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; AE000516; AAK46979.1; -; Genomic_DNA.
DR   PIR; D70726; D70726.
DR   RefSeq; WP_003413395.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WQ78; -.
DR   SMR; P9WQ78; -.
DR   PRIDE; P9WQ78; -.
DR   EnsemblBacteria; AAK46979; AAK46979; MT2666.
DR   GeneID; 45426591; -.
DR   KEGG; mtc:MT2666; -.
DR   PATRIC; fig|83331.31.peg.2873; -.
DR   HOGENOM; CLU_016922_10_0_11; -.
DR   UniPathway; UPA00733; -.
DR   Proteomes; UP000001020; 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; Transferase.
FT   CHAIN           1..449
FT                   /note="4-aminobutyrate aminotransferase"
FT                   /id="PRO_0000426823"
FT   MOD_RES         294
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   449 AA;  46813 MW;  9EB88A968B3D8719 CRC64;
     MASLQQSRRL VTEIPGPASQ ALTHRRAAAV SSGVGVTLPV FVARAGGGIV EDVDGNRLID
     LGSGIAVTTI GNSSPRVVDA VRTQVAEFTH TCFMVTPYEG YVAVAEQLNR ITPGSGPKRS
     VLFNSGAEAV ENAVKIARSY TGKPAVVAFD HAYHGRTNLT MALTAKSMPY KSGFGPFAPE
     IYRAPLSYPY RDGLLDKQLA TNGELAAARA IGVIDKQVGA NNLAALVIEP IQGEGGFIVP
     AEGFLPALLD WCRKNHVVFI ADEVQTGFAR TGAMFACEHE GPDGLEPDLI CTAKGIADGL
     PLSAVTGRAE IMNAPHVGGL GGTFGGNPVA CAAALATIAT IESDGLIERA RQIERLVTDR
     LTTLQAVDDR IGDVRGRGAM IAVELVKSGT TEPDAGLTER LATAAHAAGV IILTCGMFGN
     IIRLLPPLTI GDELLSEGLD IVCAILADL