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Database: UniProt/TrEMBL
Entry: G0G7Q5_AMYMS
LinkDB: G0G7Q5_AMYMS
Original site: G0G7Q5_AMYMS 
ID   G0G7Q5_AMYMS            Unreviewed;       430 AA.
AC   G0G7Q5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   07-JUN-2017, entry version 35.
DE   SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:AEK38690.1};
GN   OrderedLocusNames=RAM_00975 {ECO:0000313|EMBL:AEK38690.1};
OS   Amycolatopsis mediterranei (strain S699) (Nocardia mediterranei).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=713604 {ECO:0000313|EMBL:AEK38690.1, ECO:0000313|Proteomes:UP000006138};
RN   [1] {ECO:0000313|EMBL:AEK38690.1, ECO:0000313|Proteomes:UP000006138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S699 {ECO:0000313|EMBL:AEK38690.1,
RC   ECO:0000313|Proteomes:UP000006138};
RX   PubMed=21914879; DOI=10.1128/JB.05819-11;
RA   Verma M., Kaur J., Kumar M., Kumari K., Saxena A., Anand S., Nigam A.,
RA   Ravi V., Raghuvanshi S., Khurana P., Tyagi A.K., Khurana J.P., Lal R.;
RT   "Whole genome sequence of the rifamycin B-producing strain
RT   Amycolatopsis mediterranei S699.";
RL   J. Bacteriol. 193:5562-5563(2011).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP002896; AEK38690.1; -; Genomic_DNA.
DR   RefSeq; WP_013222142.1; NC_018266.1.
DR   ProteinModelPortal; G0G7Q5; -.
DR   EnsemblBacteria; AEK38690; AEK38690; RAM_00975.
DR   KEGG; amm:AMES_0188; -.
DR   KEGG; amn:RAM_00975; -.
DR   PATRIC; fig|713604.12.peg.197; -.
DR   KO; K00823; -.
DR   OMA; HSSTLYL; -.
DR   OrthoDB; POG091H0ER2; -.
DR   Proteomes; UP000006138; Chromosome.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:AEK38690.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006138};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006138};
KW   Transferase {ECO:0000313|EMBL:AEK38690.1}.
SQ   SEQUENCE   430 AA;  46133 MW;  CD3B4DB96474A760 CRC64;
     MTDELLARHR AVMPSWMSLL YEEPIEIVHA HDRRMTDSQG RTYLDFFAGV LTNSMGYDVA
     EIGDAVRKQL DTGILHTSTL YLIRSQVELA ERIAKLSNIP DAKVFFTNSG SEANDTALML
     ATQYRRSNQV LAMRNSYHGR SFATVAITGN RGWSASSLSP VKVSYVHGGY RYRSPFRTMS
     DADYIDACVA DLVDVLDTAT AGDVACLIAE PIQGVGGFSL PPDGLFRAMK EVLDEYGVLF
     ISDEVQTGWG RTGEHFWGIE AHGVTPDMMT FAKGLGNGLA VGGVVARGDV LDCFQAQSFS
     TFGGNPVSMA GATAVLDYIK DHDLQANCAA RGAQLLSGLR AAESPIVAEV RGKGLMIGVE
     LIKPGTTEPF VAAAARMLEE TKKRGLLIGK GGLHGNVLRL GPPMTLTAEE AQEGLDILVD
     ALAATHAALS
//
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