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
//