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Database: UniProt/TrEMBL
Entry: F6CKU6_DESK7
LinkDB: F6CKU6_DESK7
Original site: F6CKU6_DESK7 
ID   F6CKU6_DESK7            Unreviewed;       397 AA.
AC   F6CKU6;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   16-OCT-2013, entry version 14.
DE   SubName: Full=Aspartate transaminase;
DE            EC=2.6.1.1;
GN   OrderedLocusNames=Desku_1302;
OS   Desulfotomaculum kuznetsovii (strain DSM 6115 / VKM B-1805 / 17).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfotomaculum.
OX   NCBI_TaxID=760568;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6115 / VKM B-1805 / 17;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Lu M., Saunders E., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Nazina T.,
RA   Ivanova A., Parshina S., Kuever J., Muyzer G., Plugge C., Stams A.,
RA   Woyke T.;
RT   "Complete sequence of Desulfotomaculum kuznetsovii DSM 6115.";
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family.
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DR   EMBL; CP002770; AEG14885.1; -; Genomic_DNA.
DR   RefSeq; YP_004516686.1; NC_015573.1.
DR   EnsemblBacteria; AEG14885; AEG14885; Desku_1302.
DR   GeneID; 10665181; -.
DR   KEGG; dku:Desku_1302; -.
DR   KO; K00812; -.
DR   OMA; YAYPSVK; -.
DR   BioCyc; DKUZ760568:GHV4-1332-MONOMER; -.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Aminotransferase; Complete proteome; Pyridoxal phosphate; Transferase.
SQ   SEQUENCE   397 AA;  43305 MW;  B4C6E2D3D97E2BFF CRC64;
     MKLADRVKNI SPSPTLAIDA RAKKMIAAGE KVINFGAGEP DFDTPEHIKE AAMAAIRKGM
     TKYTPVGGTM ELKKAIIQKL KADNGLEYTP EQIVVSVGAK HSLYNAMMVL LQPGDEVILP
     APYWVTYLEQ IKLAGAVPVI VQTRQENGFK LTAEELLSVV SPRTKMVIIN SPGNPTGAVY
     AKEELVELGK VIEDRGLVVI SDEIYEKLIY DGCEHVSIAS LSPALKEQTV VINGMSKAYA
     MTGWRIGYAA APTEVARAMV DLQSHSTSNP TSVAQAASVA ALTGTQEPLR EMVAEFRRRR
     DYMLQRLNAI PGISCNTPSG AFYVFPSMGR YIGRQYKGRQ INGASDLASL LLDEVKVAVV
     PGVAFGDDRC FRLSYATSME NIVEGLNRIE QFFLQID
//
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