ID   A0PPD9_MYCUA            Unreviewed;       446 AA.
AC   A0PPD9;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   02-SEP-2026, entry version 94.
DE   RecName: Full=4-aminobutyrate aminotransferase {ECO:0000256|ARBA:ARBA00018543};
DE            EC=2.6.1.19 {ECO:0000256|ARBA:ARBA00012912};
DE            EC=2.6.1.22 {ECO:0000256|ARBA:ARBA00012876};
DE   AltName: Full=(S)-3-amino-2-methylpropionate transaminase {ECO:0000256|ARBA:ARBA00030857};
DE   AltName: Full=GABA aminotransferase {ECO:0000256|ARBA:ARBA00031787};
DE   AltName: Full=Gamma-amino-N-butyrate transaminase {ECO:0000256|ARBA:ARBA00030204};
DE   AltName: Full=Glutamate:succinic semialdehyde transaminase {ECO:0000256|ARBA:ARBA00050054};
DE   AltName: Full=L-AIBAT {ECO:0000256|ARBA:ARBA00029760};
GN   Name=gabT {ECO:0000313|EMBL:ABL04208.1};
GN   OrderedLocusNames=MUL_1723 {ECO:0000313|EMBL:ABL04208.1};
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Mycobacteriaceae; Mycobacterium; Mycobacterium ulcerans group.
OX   NCBI_TaxID=362242 {ECO:0000313|EMBL:ABL04208.1, ECO:0000313|Proteomes:UP000000765};
RN   [1] {ECO:0000313|EMBL:ABL04208.1, ECO:0000313|Proteomes:UP000000765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99 {ECO:0000313|EMBL:ABL04208.1,
RC   ECO:0000313|Proteomes:UP000000765};
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D., Davies J.K., Jenkin G.A., Small P.L., Jones L.M., Tekaia F.,
RA   Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
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         Evidence={ECO:0000256|ARBA:ARBA00001750};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde +
CC         L-glutamate; Xref=Rhea:RHEA:23352, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57706, ChEBI:CHEBI:59888; EC=2.6.1.19;
CC         Evidence={ECO:0000256|ARBA:ARBA00048021};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC       {ECO:0000256|ARBA:ARBA00005176}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP000325; ABL04208.1; -; Genomic_DNA.
DR   RefSeq; WP_011739828.1; NC_008611.1.
DR   AlphaFoldDB; A0PPD9; -.
DR   KEGG; mul:MUL_1723; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_11; -.
DR   Proteomes; UP000000765; Chromosome.
DR   GO; GO:0047298; F:(S)-3-amino-2-methylpropionate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0047589; F:5-aminovalerate:2-oxoglutarate transaminase activity; IEA:UniProtKB-ARBA.
DR   GO; GO:0042802; F:identical protein binding; IEA:TreeGrafter.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   FunFam; 3.40.640.10:FF:000013; 4-aminobutyrate aminotransferase; 1.
DR   FunFam; 3.90.1150.10:FF:000022; 4-aminobutyrate aminotransferase; 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; IPR050103; Class-III_PLP-dep_AT.
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   NCBIfam; NF004714; PRK06058.1; 1.
DR   PANTHER; PTHR11986:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 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   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:ABL04208.1};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000765};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   446 AA;  47215 MW;  A175CE8FC1224760 CRC64;
     MASLDQSRLL VTEIPGPASL ELNKRRAAAV SGGVGVTLPV FVVRAGGGIV EDADGNRLID
     LGSGIAVTTI GNSAPRVVDA VRDQVEQFTH TCFMVIPYEH YVAVAEQLNR ITPGSGEKRT
     VLFNSGAEAV ENSIKVARAH TRKQAVVAFD YAYHGRTNLT MALTAKSMPY KSGFGPFAPE
     IYRAPVSYPY RDNLLDKDIA TDGELAAERA INLIDKQIGA ANLAAVIIEP IAGEGGFIVP
     ADGFLPALQR WSRDNDVVFI ADEVQTGFAR TGAMFACDHE NVEPDLIVTA KGIADGFPLS
     AVTGRAEIMD APHTSGLGGT FGGNPVACAA ALATIETIER DGMVERARQI ERLVMDRLLR
     LQAADDRLGD VRGRGAMIAM ELVKSGTAEP DAALTQKLAA AAHAAGVIVL TCGMFGNVIR
     LLPPLTISDE LLSEGLDILC QILADL
//