ID   A0QV88_MYCS2            Unreviewed;       417 AA.
AC   A0QV88;
DT   09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 109.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ABK71148.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:ABK71148.1};
GN   OrderedLocusNames=MSMEG_2487 {ECO:0000313|EMBL:ABK71148.1};
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK71148.1, ECO:0000313|Proteomes:UP000000757};
RN   [1] {ECO:0000313|EMBL:ABK71148.1, ECO:0000313|Proteomes:UP000000757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) 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|RuleBase:RU003560}.
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DR   EMBL; CP000480; ABK71148.1; -; Genomic_DNA.
DR   RefSeq; WP_011728377.1; NZ_SIJM01000012.1.
DR   RefSeq; YP_886826.1; NC_008596.1.
DR   AlphaFoldDB; A0QV88; -.
DR   STRING; 246196.MSMEG_2487; -.
DR   PaxDb; 246196-MSMEI_2427; -.
DR   GeneID; 66733899; -.
DR   KEGG; msm:MSMEG_2487; -.
DR   PATRIC; fig|246196.19.peg.2452; -.
DR   eggNOG; COG0160; Bacteria.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000000757; Chromosome.
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   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; 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   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:ABK71148.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000757};
KW   Transferase {ECO:0000313|EMBL:ABK71148.1}.
SQ   SEQUENCE   417 AA;  43922 MW;  28756732FA1A644D CRC64;
     MTELSQALKQ ATGVIAARGE GVLLYDEQDR RYLDFTAGIG VTSTGHCHPR VVEAAQRQVG
     TLIHGQYTTV MHRPLLTLVE RLGEVLPAGL DRMFFANSGS EAIEAALRLS RQATGRPNVI
     VFHGGFHGRT VAAASMTTSG TKFRSGFSPL MAGVHVSPFP DPTHFGWPVE QTTDFALSQL
     DYVLQTVSAP ADTAAFFVEP VLGEGGYVPA NERFLAGLRE RADAHGILLV LDEVQTGYGR
     TGKFWGGEHF DAKPDILVTA KGLASGFPLS GIAASSELMA KAWPGSQGGT YGANAVACAA
     AIATLDVIAD ENLVANAAER GAQLKQALQT VADKHEQITD VRGLGLMIGN EFRDADGKPD
     GTTAAAVQQE AARRGLLLLT CGAWGQVVRF IPALVVSADE VEEAAGIWAD AVSAVVS
//