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Database: UniProt/TrEMBL
Entry: D2PZE2_KRIFD
LinkDB: D2PZE2_KRIFD
Original site: D2PZE2_KRIFD 
ID   D2PZE2_KRIFD            Unreviewed;       429 AA.
AC   D2PZE2;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   07-JUN-2017, entry version 45.
DE   SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ADB33751.1};
GN   OrderedLocusNames=Kfla_4734 {ECO:0000313|EMBL:ADB33751.1};
OS   Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399).
OC   Bacteria; Actinobacteria; Propionibacteriales; Nocardioidaceae;
OC   Kribbella.
OX   NCBI_TaxID=479435 {ECO:0000313|EMBL:ADB33751.1, ECO:0000313|Proteomes:UP000007967};
RN   [1] {ECO:0000313|Proteomes:UP000007967}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17836 / JCM 10339 / NBRC 14399
RC   {ECO:0000313|Proteomes:UP000007967};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K.,
RA   Ivanova N., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Pukall R., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Kribbella flavida DSM 17836.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP001736; ADB33751.1; -; Genomic_DNA.
DR   RefSeq; WP_012922305.1; NC_013729.1.
DR   ProteinModelPortal; D2PZE2; -.
DR   STRING; 479435.Kfla_4734; -.
DR   EnsemblBacteria; ADB33751; ADB33751; Kfla_4734.
DR   KEGG; kfl:Kfla_4734; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K00823; -.
DR   OMA; HSSTLYL; -.
DR   OrthoDB; POG091H0APS; -.
DR   BioCyc; KFLA479435:GI0F-4660-MONOMER; -.
DR   Proteomes; UP000007967; 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:ADB33751.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007967};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007967};
KW   Transferase {ECO:0000313|EMBL:ADB33751.1}.
SQ   SEQUENCE   429 AA;  46416 MW;  1F887AE906A1A527 CRC64;
     MTHAELWERH RAVMPDWLAL YYEEPIEIVS GSGRRVTDGE GNQYLDFFAG ILTNAIGYDV
     AEISDAVREQ LATGVAHTST VYLIRRQIEL AERIAELSGI KEAKVFFTNS GTEANEAALL
     LATQQRRSNQ VLAMRNSYHG RSFGTIAITG HRGWSASSLS PVNVQYVQGA YRYRSPFRDL
     PDAEYIKVCV EDLRTVIDTT TSGDVACLIA EPIQGVGGFA SPPDGLFAAF KEVLDEYGIL
     LISDEVQTGW GRTGEHFWGI QAHDVVPDAM TFAKGLGNGF AIGGVVATPA MMDSLSANSL
     STFGGNPIAT TAAKATLEYL LDKDLQANAA KRGAQLADGL RGIADEFPEL GDVRGKGLML
     AAEIVRPDDR VPDAATTAKL QQEAKNRGLL IGKGGLYGNV LRMAPPMTLT EPETTEAIEI
     LRDSFNTLR
//
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