ID   Q0RCW9_FRAAA            Unreviewed;       473 AA.
AC   Q0RCW9;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=4-aminobutyrate aminotransferase, PLP-dependent {ECO:0000313|EMBL:CAJ64705.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:CAJ64705.1};
GN   Name=gabT {ECO:0000313|EMBL:CAJ64705.1};
GN   OrderedLocusNames=FRAAL6081 {ECO:0000313|EMBL:CAJ64705.1};
OS   Frankia alni (strain DSM 45986 / CECT 9034 / ACN14a).
OC   Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=326424 {ECO:0000313|EMBL:CAJ64705.1, ECO:0000313|Proteomes:UP000000657};
RN   [1] {ECO:0000313|EMBL:CAJ64705.1, ECO:0000313|Proteomes:UP000000657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACN14a {ECO:0000313|Proteomes:UP000000657};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N., Couloux A.,
RA   Cournoyer B., Cruveiller S., Daubin V., Demange N., Francino M.P.,
RA   Goltsman E., Huang Y., Kopp O.R., Labarre L., Lapidus A., Lavire C.,
RA   Marechal J., Martinez M., Mastronunzio J.E., Mullin B.C., Niemann J.,
RA   Pujic P., Rawnsley T., Rouy Z., Schenowitz C., Sellstedt A., Tavares F.,
RA   Tomkins J.P., Vallenet D., Valverde C., Wall L.G., Wang Y., Medigue C.,
RA   Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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; CT573213; CAJ64705.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0RCW9; -.
DR   STRING; 326424.FRAAL6081; -.
DR   KEGG; fal:FRAAL6081; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_11; -.
DR   Proteomes; UP000000657; 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   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:CAJ64705.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000657};
KW   Transferase {ECO:0000313|EMBL:CAJ64705.1}.
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   473 AA;  49038 MW;  A912B82E6011A5CB CRC64;
     MPWWTAAGEQ AGADEMNPPN VPARGGPGLP QIRRLVTEIP GPRSRALAAR RAGAVARGVG
     ETLPVYVHAA GGGVVVDVDG NSLIDFGSGI AVVSVGNAAD GVVAAVREQV GRFTHTCFMI
     TPYEGYVAVC EALNRLTPGD HDKRSALFNS GAEAVENAVK IARSATGRAA IVVFEHAYHG
     RTNLTLAMTA KSAPYKAGFG PFAPEVYRVP LAYPYRWPTG REHCGEQAAA RVIELVRDEI
     GAGEVAALVI EPIQGEGGFI VPGRGFLPRL AEFCADAGIL FVADEIQTGF ARTGTMFACE
     DEGVVPDLIT TAKGIAGGMP LAAVTGRAEI MDAPQVGGLG GTYGGNPAAC AAALAAIGFI
     ESADLAARAR RIGELALPRL RALAARYDVI GDVRGRGAML ALELVRGGGD TRPDRELTGA
     VAAACHRRGL IVLTAGTWGN VLRLLPPLVM DPALLLAGLD VLDEAFAEVT AAR
//