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Database: UniProt
Entry: A0A100W2U0_9MYCO
LinkDB: A0A100W2U0_9MYCO
Original site: A0A100W2U0_9MYCO 
ID   A0A100W2U0_9MYCO        Unreviewed;       450 AA.
AC   A0A100W2U0;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:GAS90598.1};
GN   ORFNames=RMCB_4694 {ECO:0000313|EMBL:GAS90598.1};
OS   Mycolicibacterium brisbanense.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=146020 {ECO:0000313|EMBL:GAS90598.1, ECO:0000313|Proteomes:UP000069620};
RN   [1] {ECO:0000313|EMBL:GAS90598.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM15654 {ECO:0000313|EMBL:GAS90598.1};
RA   Katahira K., Ogura Y., Gotoh Y., Hayashi T.;
RT   "Draft Genome Sequences of Five Rapidly Growing Mycobacterium Species, M.
RT   thermoresistibile, M. fortuitum subsp. acetamidolyticum, M. canariasense,
RT   M. brisbanense, and M. novocastrense.";
RL   Genome Announc. 4:e00322-16(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAS90598.1}.
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DR   EMBL; BCSX01000040; GAS90598.1; -; Genomic_DNA.
DR   RefSeq; WP_062830696.1; NZ_JACKTM010000079.1.
DR   AlphaFoldDB; A0A100W2U0; -.
DR   STRING; 146020.RMCB_4694; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000069620; Unassembled WGS sequence.
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   PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 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:GAS90598.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:GAS90598.1}.
SQ   SEQUENCE   450 AA;  47601 MW;  0B22CBB4874D00E8 CRC64;
     MTVVDTRQDR PSSVRRIVTA IPGPRSVELA ARRSAALPAG LTSSSVVYAE RAGDGVLVDV
     DGNSFIDLGS GIAVTTVGNS APRVVERAAA QLERFTHTCF LVNGYESYVE VCETLNRLTP
     GDHQKRTALF NTGAEAVENA VKYARVATGR PAVVVFDHAF HGRSLLTMTM TAKNMPYKNN
     FGPFAPEVYR VPMAYPYRWP SGPDNAAAEA FEEFRLVVDT QIGAGSVAAV VVEPIQGEGG
     FIVPAPGFLR QVAEFCAERG ILLIADEVQT GIARTGHWFA SEHEGIVPDL ITTAKGLGGG
     LPLAAVTGRA EVMDAAHAGG IGGTYSGNPV ACEAALGVFE TIESEDLLGR ARRIGEILQS
     ELTDIAAGTK VIGDIRGRGA MIAAEFVTDD AVTPNRDAVA EIVRYAQDNG VLTLTAGTFG
     NVLRFLPPLT IPDDLLREGL GVIRDAVARI
//
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