ID A0A024JX14_9MYCO Unreviewed; 446 AA.
AC A0A024JX14;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:CDO88171.1};
GN Name=gabT {ECO:0000313|EMBL:CDO88171.1};
GN ORFNames=BN973_02535 {ECO:0000313|EMBL:CDO88171.1};
OS Mycobacterium triplex.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium simiae complex.
OX NCBI_TaxID=47839 {ECO:0000313|EMBL:CDO88171.1};
RN [1] {ECO:0000313|EMBL:CDO88171.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO88171.1};
RX PubMed=24874681; DOI=10.1128/genomeA.00499-14;
RA Sassi M., Croce O., Robert C., Raoult D., Drancourt M.;
RT "Draft Genome Sequence of Mycobacterium triplex DSM 44626.";
RL Genome Announc. Announc.2:e00499-e00414(2014).
RN [2] {ECO:0000313|EMBL:CDO88171.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 44626 {ECO:0000313|EMBL:CDO88171.1};
RA Urmite Genomes U.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; HG964446; CDO88171.1; -; Genomic_DNA.
DR RefSeq; WP_036468456.1; NZ_LQPY01000034.1.
DR AlphaFoldDB; A0A024JX14; -.
DR STRING; 47839.BN973_02535; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_11; -.
DR OrthoDB; 9801052at2; -.
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; 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 Aminotransferase {ECO:0000313|EMBL:CDO88171.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:CDO88171.1}.
SQ SEQUENCE 446 AA; 46825 MW; 5007BA53E137E64D CRC64;
MASLEQTRQL VTEIPGPKSL ELDKRRTSAV SAGVGVTLPV YVARAGGGIV EDVDGNRLID
LGSGIAVTTI GNSAPRVVDA VREQVAEFTH TCFMVTPYQS YVAVAEELNR ITPGSGEKRS
VLFNSGAEAV ENSVKIARSY TRKTAVAAFD HAYHGRTNMA MALTAKSMPY KSGFGPFAPE
IYRAPMSYPY RDGLLDKDLA TDGELAAARA ISVLDKQIGA ANLAAVIIEP IQGEGGFIVP
AEGFLPALVD WCRKNNVVFI ADEVQSGFAR TGAMFACEHE GIEPDLICTA KGIAGGLPLS
AVTGRAEIMD APHVSGLGGT FGGNPVACAA ALASIATIEN DGLIERAQQI ERLITDVLLR
MQAGDDRIGD VRGRGAMIAV ELVKSGTSEP DAELTNKLAT AAGAAGVIVL TCGMYGNIVR
LLPPLTISDE LLTEGLEVLR LLLADL
//