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Database: UniProt/TrEMBL
Entry: U5W3Q6_9ACTN
LinkDB: U5W3Q6_9ACTN
Original site: U5W3Q6_9ACTN 
ID   U5W3Q6_9ACTN            Unreviewed;       433 AA.
AC   U5W3Q6;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   07-JUN-2017, entry version 20.
DE   SubName: Full=Class III aminotransferase {ECO:0000313|EMBL:AGZ43769.1};
GN   ORFNames=AFR_27540 {ECO:0000313|EMBL:AGZ43769.1};
OS   Actinoplanes friuliensis DSM 7358.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Actinoplanes.
OX   NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ43769.1, ECO:0000313|Proteomes:UP000017746};
RN   [1] {ECO:0000313|EMBL:AGZ43769.1, ECO:0000313|Proteomes:UP000017746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ43769.1,
RC   ECO:0000313|Proteomes:UP000017746};
RX   PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA   Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA   Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT   "Complete genome sequence of the actinobacterium Actinoplanes
RT   friuliensis HAG 010964, producer of the lipopeptide antibiotic
RT   friulimycin.";
RL   J. Biotechnol. 178:41-42(2014).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP006272; AGZ43769.1; -; Genomic_DNA.
DR   ProteinModelPortal; U5W3Q6; -.
DR   EnsemblBacteria; AGZ43769; AGZ43769; AFR_27540.
DR   KEGG; afs:AFR_27540; -.
DR   PATRIC; fig|1246995.3.peg.5582; -.
DR   KO; K00823; -.
DR   OrthoDB; POG091H0ER2; -.
DR   Proteomes; UP000017746; 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:AGZ43769.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000017746};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017746};
KW   Transferase {ECO:0000313|EMBL:AGZ43769.1}.
SQ   SEQUENCE   433 AA;  46117 MW;  FC6C44F011ACDE27 CRC64;
     MTDDLLARHQ AVMPSWVTTY YGDNAIELVS GSGRRVTDAA GRTYLDFFGG VLTNMLGYDI
     AEVREAVERQ LATGIVHSST LYLIRQQVEL AEKIARVSGI PDARVFFTNS GTEANEAALL
     FTTNHRRSNQ ILAIRNSYHG RSFAAMAITG HRSWSASALS PVSVSWLNSG ERLRGRMKGL
     SDADHIDAAV EDLREVLATT TSGDVAALIA EPIQGVGGFV HAPDGLLGAL KKELDNHGIL
     LIADEVQTGW GRTGDHFWGY QAHDVQPDLI TFAKGIGNGF ALAGVVGRAE LVNAVPATSF
     STFGGNPIST AAGNAVLDYV LDHDLQANAA RTGTILLDGL RAALGDTKIV GEIRGRGLMI
     GIEFVRPGTT DPDTAATMRV FDECRKGGLL VGKGGLYGNV LRMGPPLTLT EDEAREGLAI
     LTEAIRTADA ESF
//
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