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Database: UniProt
Entry: A0A3M8AAV6_9MICO
LinkDB: A0A3M8AAV6_9MICO
Original site: A0A3M8AAV6_9MICO 
ID   A0A3M8AAV6_9MICO        Unreviewed;       452 AA.
AC   A0A3M8AAV6;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=4-aminobutyrate--2-oxoglutarate transaminase {ECO:0000313|EMBL:RNB48380.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:RNB48380.1};
GN   Name=gabT {ECO:0000313|EMBL:RNB48380.1};
GN   ORFNames=EDM22_11170 {ECO:0000313|EMBL:RNB48380.1};
OS   Agromyces tardus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Agromyces.
OX   NCBI_TaxID=2583849 {ECO:0000313|EMBL:RNB48380.1, ECO:0000313|Proteomes:UP000275048};
RN   [1] {ECO:0000313|EMBL:RNB48380.1, ECO:0000313|Proteomes:UP000275048}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJ-23 {ECO:0000313|EMBL:RNB48380.1,
RC   ECO:0000313|Proteomes:UP000275048};
RA   Sun T.;
RT   "Isolation, diversity and antibacterial activity of antinobacteria from the
RT   wheat rhizosphere soil.";
RL   Submitted (OCT-2018) 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}.
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:RNB48380.1}.
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DR   EMBL; RHHB01000020; RNB48380.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M8AAV6; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000275048; Unassembled WGS sequence.
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:RNB48380.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000275048};
KW   Transferase {ECO:0000313|EMBL:RNB48380.1}.
SQ   SEQUENCE   452 AA;  46408 MW;  C5CEA24FD4B046A0 CRC64;
     MTLVAPTATT VGGPALPQER RLVTSIPGPR SQELMARKAE AVAAGVGTTI PVSVVAAGGG
     VIVDADGNSI IDLGSGIAVT GVGNSNPRVV EAVTAQLNAF THTCFTVAPY DGYVSVAEKL
     NELTPGDHAK RSALFNSGAE AVENAVKIAR HYTKKQAVVA FDHAYHGRTN LTMGLTAKNI
     PYKSGFGPFA PEVYRAPLSY PFRDGGLSGA EAAARAILQI EKQVGAENLA AIIIEPIQGE
     GGFIVPAPGF LPALVKWANE NDVVFIADEV QTGFGRTGAW FASEHEGIVP DVIVTAKGIA
     GGLPLSAVTG RAEIMDSAMA GGLGGTYAGS PIACAAALAA IESYREDGLI ERAREIGTVL
     IGRLNALRTA DARIGDVRGR GAMVAIELVD PATGAPDAAL TGKLAAYAAQ HGVLVLTCGT
     YGNVIRFLPP LTISDELLIE GLGVIAEGLK QA
//
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