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Database: UniProt/TrEMBL
Entry: A0A0U3ENL6_9ACTN
LinkDB: A0A0U3ENL6_9ACTN
Original site: A0A0U3ENL6_9ACTN 
ID   A0A0U3ENL6_9ACTN        Unreviewed;       444 AA.
AC   A0A0U3ENL6;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ALV33009.1};
GN   ORFNames=AS200_13785 {ECO:0000313|EMBL:ALV33009.1};
OS   Streptomyces sp. CdTB01.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1725411 {ECO:0000313|EMBL:ALV33009.1, ECO:0000313|Proteomes:UP000068029};
RN   [1] {ECO:0000313|EMBL:ALV33009.1, ECO:0000313|Proteomes:UP000068029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CdTB01 {ECO:0000313|EMBL:ALV33009.1,
RC   ECO:0000313|Proteomes:UP000068029};
RA   Tian Y., Zhou G., Yang H., Lu X.;
RT   "Complete genome sequence of the Streptomyces sp. strain CdTB01, a
RT   bacterium tolerant to cadmium.";
RL   Submitted (DEC-2015) 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; CP013743; ALV33009.1; -; Genomic_DNA.
DR   RefSeq; WP_058922686.1; NZ_CP013743.1.
DR   AlphaFoldDB; A0A0U3ENL6; -.
DR   STRING; 1725411.AS200_13785; -.
DR   KEGG; scx:AS200_13785; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000068029; Chromosome.
DR   GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
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; 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:ALV33009.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000068029};
KW   Transferase {ECO:0000313|EMBL:ALV33009.1}.
SQ   SEQUENCE   444 AA;  46455 MW;  7AF61C605494B947 CRC64;
     MSALPQERRV VTAIPGPKSQ ELQARRTAAV AQGVGSVLPV FTARAGGGII EDVDGNRLID
     FGSGIAVTSV GASAEAVVRR ASAQLADFTH TCFMVTPYEG YVAVAEALAE LTPGDHAKKS
     ALFNSGAEAV ENAVKIARAY TKRQAVVVFD HGYHGRTNLT MALTAKNMPY KHGFGPFAPE
     VYRVPVAYGY RWPTGPENAG PEAAAQAIDQ ITKQVGPENV AAIIIEPVLG EGGFIEPAKG
     FLPAISKFAS DNGIVFVADE IQSGFCRTGQ WFACEDEGIV PDLITTAKGI AGGLPLAAVT
     GRAEIMDAAH AGGLGGTYGG NPVACAGALG AIETMKELDL NARAKDIEAV MKARLTAMAE
     KFDVIGDVRG RGAMIAIELV KDRATKEPNP EATAALAKAC HQEGLLVLTC GTYGNVLRFL
     PPLVIGEDLL NEGLDIIEQA FARI
//
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