ID   Q0S806_RHOJR            Unreviewed;       413 AA.
AC   Q0S806;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 106.
DE   SubName: Full=4-aminobutyrate transaminase {ECO:0000313|EMBL:ABG96330.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:ABG96330.1};
GN   Name=gabT2 {ECO:0000313|EMBL:ABG96330.1};
GN   OrderedLocusNames=RHA1_ro04544 {ECO:0000313|EMBL:ABG96330.1};
OS   Rhodococcus jostii (strain RHA1).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Rhodococcus.
OX   NCBI_TaxID=101510 {ECO:0000313|EMBL:ABG96330.1, ECO:0000313|Proteomes:UP000008710};
RN   [1] {ECO:0000313|Proteomes:UP000008710}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA1 {ECO:0000313|Proteomes:UP000008710};
RX   PubMed=17030794; DOI=10.1073/pnas.0607048103;
RA   McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C.,
RA   Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H.,
RA   Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H.,
RA   Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R.,
RA   Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W.,
RA   Eltis L.D.;
RT   "The complete genome of Rhodococcus sp. RHA1 provides insights into a
RT   catabolic powerhouse.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006).
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; CP000431; ABG96330.1; -; Genomic_DNA.
DR   RefSeq; WP_011596921.1; NC_008268.1.
DR   AlphaFoldDB; Q0S806; -.
DR   KEGG; rha:RHA1_ro04544; -.
DR   PATRIC; fig|101510.16.peg.4580; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_11; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000008710; 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   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:ABG96330.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008710};
KW   Transferase {ECO:0000313|EMBL:ABG96330.1}.
SQ   SEQUENCE   413 AA;  43577 MW;  5B22C27382AF31E0 CRC64;
     MTRLSPLLAQ ATPVTVDHGE GCYLYGTDGR RYLDFTAGIG VTSTGHCHPH VVEAARRQIG
     SLIHGQYTTV MHQPMLELVD RLGSVLPAGL DSLFFANSGS EAVEASLRLS RQATGRPNVI
     VFHGGFHGRT VATATMTTSG TRFSAGFSPL MGGVHVAPFP NAYRYGWSEE EATAFALKEL
     DYIFATLTAP NETAAFVVEP VLGEGGYVPG NTAFFQGLRE RADRYGILLV IDEIQTGFGR
     TGKFFGHQHF DVRPDIITIA KGLASGFPLS GIAASEALMA KGWPGSQGGT YGGNAVSCAA
     AVATLEVIEK EDLVANAAAR GVQLLDGART RAIDGIGDVR GLGLLVGSEF TAADGSADRT
     KASAAQQLAA KKGLLLLTCG AHMNVVRMIP PLIVTAEQIE DALKIWSEVL DEV
//