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Database: UniProt
Entry: A0A0C1XQI6_9ACTN
LinkDB: A0A0C1XQI6_9ACTN
Original site: A0A0C1XQI6_9ACTN 
ID   A0A0C1XQI6_9ACTN        Unreviewed;       444 AA.
AC   A0A0C1XQI6;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:KIF77018.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:KIF77018.1};
GN   ORFNames=QR77_30530 {ECO:0000313|EMBL:KIF77018.1};
OS   Streptomyces sp. 150FB.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF77018.1, ECO:0000313|Proteomes:UP000031584};
RN   [1] {ECO:0000313|EMBL:KIF77018.1, ECO:0000313|Proteomes:UP000031584}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=150FB {ECO:0000313|EMBL:KIF77018.1,
RC   ECO:0000313|Proteomes:UP000031584};
RA   Tarkka M.T., Feldhahn L., Kruger D., Buscot F., Wubet T.;
RT   "Genome sequence of the mycoparasite antagonist Streptomyces sp. strain FB
RT   150.";
RL   Submitted (NOV-2014) 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:KIF77018.1}.
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DR   EMBL; JTHL01000001; KIF77018.1; -; Genomic_DNA.
DR   RefSeq; WP_040025225.1; NZ_JTHL01000001.1.
DR   AlphaFoldDB; A0A0C1XQI6; -.
DR   STRING; 1576605.QR77_30530; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000031584; 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:0009058; P:biosynthetic process; IEA:UniProt.
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; 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; ORNITHINE AMINOTRANSFERASE; 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:KIF77018.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031584};
KW   Transferase {ECO:0000313|EMBL:KIF77018.1}.
SQ   SEQUENCE   444 AA;  46489 MW;  6C7406C515361CEF CRC64;
     MTAIPQERRL VTAIPGPKSQ ELQARRIATV AGGVGSTMPV FAARAGGGVL EDVDGNRLID
     FGSGIAVTTV GNSAEAVVRR ASAQLADFTH TCFMVTPYEG YVAVCEQLAE LTPGDHAKKS
     ALFNSGAEAV ENAVKIARIH TKRQAVVVFD HGYHGRTNLT MALTSKNMPY KNGFGPFAPE
     IYRVPVAYPY RWPTGAENCG AEASAQAIDQ ISKQIGAENV AAIIIEPVLG EGGFIEPAKG
     FLPALAAFAK DNGIVFVADE IQSGFCRTGQ WFACENEGIV PDLITTAKGI AGGLPLAAVT
     GRAEIMDAAH SGGLGGTYGG NPVACAAALG AIETMKELDL PAKAVHIEQI MKPRLAAMQE
     KYDVIGDVRG RGGMIAIELV KDRTTKEPAP EATAALAKAC HTEGLLVLVT GTYGNVLRFL
     PPLVIGDDLL NEGLDILEQA LAGI
//
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