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Database: UniProt/TrEMBL
Entry: D6Y7T4_THEBD
LinkDB: D6Y7T4_THEBD
Original site: D6Y7T4_THEBD 
ID   D6Y7T4_THEBD            Unreviewed;       431 AA.
AC   D6Y7T4;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   07-JUN-2017, entry version 42.
DE   SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ADG87753.1};
GN   OrderedLocusNames=Tbis_1030 {ECO:0000313|EMBL:ADG87753.1};
OS   Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 /
OS   JCM 10125 / NBRC 14880 / R51).
OC   Bacteria; Actinobacteria; Actinobacteria incertae sedis;
OC   Thermobispora.
OX   NCBI_TaxID=469371 {ECO:0000313|EMBL:ADG87753.1, ECO:0000313|Proteomes:UP000006640};
RN   [1] {ECO:0000313|EMBL:ADG87753.1, ECO:0000313|Proteomes:UP000006640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / NBRC 14880 /
RC   R51 {ECO:0000313|Proteomes:UP000006640};
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., Mikhailova N., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA   Hugenholtz P., Woyke T., Wu D., Jando M., Schneider S., Klenk H.-P.,
RA   Eisen J.A.;
RT   "The complete genome of Thermobispora bispora DSM 43833.";
RL   Submitted (JAN-2010) 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; CP001874; ADG87753.1; -; Genomic_DNA.
DR   RefSeq; WP_013131286.1; NC_014165.1.
DR   ProteinModelPortal; D6Y7T4; -.
DR   STRING; 469371.Tbis_1030; -.
DR   EnsemblBacteria; ADG87753; ADG87753; Tbis_1030.
DR   KEGG; tbi:Tbis_1030; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K00823; -.
DR   OMA; HSSTLYL; -.
DR   OrthoDB; POG091H0ER2; -.
DR   BioCyc; TBIS469371:GHSI-1037-MONOMER; -.
DR   Proteomes; UP000006640; 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:ADG87753.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006640};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006640};
KW   Transferase {ECO:0000313|EMBL:ADG87753.1}.
SQ   SEQUENCE   431 AA;  46232 MW;  E36EA6DBD0CFDD86 CRC64;
     MPDLLARHRA VMPKWMTLYY DEPIEIVSGK GCRVVDSTGK SYLDFFAGIL TNMIGYDIPE
     VKEAVERQLA TGVVHTSTLY LIRGQVELAE KIARLSGIPN AKVFFTNSGT EANETALLLA
     TYARGTDQVL AMRQSYHGRS FGAISVTSNR AWKNNSLSPL NVHFLHGADR HLPQFRGMSD
     EEYIAACVAD LRHVLATVAA GKVAALIAEP IQGVGGFTMA PDGLFAAYKE VLDEEGILFI
     SDEVQTGWGR TGSAFFGIQN HGVTPDMITF AKGIGNGFAV GGVVARGDLM DAPHAIGLST
     FGGNPIAMTA ANATLDYVLD HDLQANAARM GDIIIPGLRE AARRLPIVGD VRGKGLMFAI
     DLVDPATREP SPPLAARFME ETKKRGLLVG KGGLYGHTVR MAPPLTLSEE EAREGLGIIV
     AALEAINDEA R
//
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