ID   Q47S39_THEFY            Unreviewed;       448 AA.
AC   Q47S39;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AAZ54728.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:AAZ54728.1};
GN   OrderedLocusNames=Tfu_0690 {ECO:0000313|EMBL:AAZ54728.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54728.1};
RN   [1] {ECO:0000313|EMBL:AAZ54728.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=YX {ECO:0000313|EMBL:AAZ54728.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of Thermobifida fusca YX.";
RL   Submitted (JUL-2005) 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; CP000088; AAZ54728.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q47S39; -.
DR   STRING; 269800.Tfu_0690; -.
DR   KEGG; tfu:Tfu_0690; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_11; -.
DR   OrthoDB; 3204291at2; -.
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   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:AAZ54728.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:AAZ54728.1}.
SQ   SEQUENCE   448 AA;  47402 MW;  EC31547F8DEDC3D1 CRC64;
     MASEHADLPQ ERRLVTEIPG PRSRALQERR TAAVAQGVGS SLPVYVVRAS GGIVEDVDGN
     RLIDFGSGIA VTNVGNANPR VVARASEQLA RFTHTCFMIN PYEGYVDVCE ALNRITPGDH
     EKRSILVNSG AEAVENAVKI ARHATGRQAV VVFDHAYHGR TNLTMALTAR NMPYKQGFGP
     FAGEVYRMPM AYPFRWPTGP DNCGPEAAAQ AIDLITTQIG PENVAAVLIE PIQGEGGFIV
     PGEGFLPALV EFCRKHGIVF IADEIQTGFA RTGRLFACEH EGIVPDLITT AKGIAGGLPL
     AAVTGRAELM DAVHGGGLGG TYGGNPVACA AALAALETIE QDNLVERARA IGDVLLSRLR
     ALAERYDIIG DVRGRGAMVA MELVAGAGDK TPNPEALASV VKYCHAKGLI LLTAGTYGNV
     IRLLPPLVIS DALLDEGLTI IEEAFAQL
//