ID   Q741P8_MYCPA            Unreviewed;       449 AA.
AC   Q741P8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=GabT {ECO:0000313|EMBL:AAS03358.1};
GN   Name=gabT {ECO:0000313|EMBL:AAS03358.1};
GN   OrderedLocusNames=MAP_1041c {ECO:0000313|EMBL:AAS03358.1};
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316 {ECO:0000313|EMBL:AAS03358.1, ECO:0000313|Proteomes:UP000000580};
RN   [1] {ECO:0000313|EMBL:AAS03358.1, ECO:0000313|Proteomes:UP000000580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10 {ECO:0000313|Proteomes:UP000000580};
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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; AE016958; AAS03358.1; -; Genomic_DNA.
DR   RefSeq; WP_003872681.1; NZ_CP106873.1.
DR   AlphaFoldDB; Q741P8; -.
DR   STRING; 262316.MAP_1041c; -.
DR   KEGG; mpa:MAP_1041c; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_11; -.
DR   Proteomes; UP000000580; Chromosome.
DR   GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
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   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000580}.
SQ   SEQUENCE   449 AA;  47321 MW;  4A96C4ACB479059F CRC64;
     MARLEQTRRL VTEIPGPASL ELSKRRAAAV SHAVNVSVPV FVARAGGGIV EDVDGNRLID
     LGSGIAVTTI GNSAPRVVDA VRAQVAEFTH TCFMVTPYES YVAVAEMLNR ITPGAGDKRS
     VLFNSGAEAV ENAVKVARAY TRKPAVVAFD HAYHGRTNLA MALTAKSMPY KGGFGPFAPE
     IYRAPLSYPY RDGLLDKELA TDGEKAAARA INIIDGQIGA DSLAAVIIEP IQGEGGFIVP
     VEGFLPTLLD WCRRNDVLFI ADEVQTGFAR SGAMFACEHE GPNGLEPDLI CTAKAIADGL
     PLSAVTGRAQ IMDAPHVGGL GGTFGGNPLA CAAALATIET IESDGLIERA RQLERLITEP
     LLRLQARDDR IGDVRGRGAM IAIELVKSGT AEPDKDLTQR LSVAAHAAGV IVLTCGMFGN
     IIRLLPPLTI SDELLAEGID ILGGLLADL
//