GenomeNet

Database: UniProt
Entry: D7C260_STRBB
LinkDB: D7C260_STRBB
Original site: D7C260_STRBB 
ID   D7C260_STRBB            Unreviewed;       454 AA.
AC   D7C260;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Aminotransferase {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=SBI_00593 {ECO:0000313|EMBL:ADI03714.1};
OS   Streptomyces bingchenggensis (strain BCW-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI03714.1, ECO:0000313|Proteomes:UP000000377};
RN   [1] {ECO:0000313|EMBL:ADI03714.1, ECO:0000313|Proteomes:UP000000377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCW-1 {ECO:0000313|EMBL:ADI03714.1,
RC   ECO:0000313|Proteomes:UP000000377};
RX   PubMed=20581206; DOI=10.1128/JB.00596-10;
RA   Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA   Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA   Xiang W.S.;
RT   "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT   bingchenggensis.";
RL   J. Bacteriol. 192:4526-4527(2010).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002047; ADI03714.1; -; Genomic_DNA.
DR   RefSeq; WP_014173193.1; NC_016582.1.
DR   AlphaFoldDB; D7C260; -.
DR   STRING; 749414.SBI_00593; -.
DR   KEGG; sbh:SBI_00593; -.
DR   PATRIC; fig|749414.3.peg.609; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_4_0_11; -.
DR   Proteomes; UP000000377; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
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; 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   PANTHER; PTHR43094; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR43094:SF1; AMINOTRANSFERASE CLASS-III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000377}.
SQ   SEQUENCE   454 AA;  49357 MW;  AFA0C4C96573811C CRC64;
     MTLVHPELNP QAIARTYELD RRHVFHSWSA QAEITPMVIT RAEGSYIWDG EGNRLLDFSS
     QLVNTNIGHQ HPYVVEAIAD QARTLATVAP QHANDQRSEA ARLICERAPG ELNRVFFTNG
     GADANEHAVR MARLTTGRPK VLSRYRSYHG GTQTAINLTG DPRRWPNDEG TSGVVHFFGP
     YLYRSHFDAT TEEEECRRAL AHLEQVIELE GPQTIAAILL EAIPGTAGIM PPPPGYLAGV
     RALCDQYGIV FIVDEVMTGF GRTGAWFVCD DEGVVPDLLT FAKGVNSGYV PLGGVVISDR
     IAEHFAHRPY PGGLTYSGHP LACAAAVAAI TVMERDGIID NARRIGTDVF GPELVRLAAQ
     HPSVGEVRGR GVFWAIELVT DRHTRRPVAP TGGSSPVMAE AVRASKELGL LPFTNSGRIH
     LVPPCTITES EAREGLHIID QVLSRVDTLC GASS
//
DBGET integrated database retrieval system