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Database: UniProt/TrEMBL
Entry: Q47S43_THEFY
LinkDB: Q47S43_THEFY
Original site: Q47S43_THEFY 
ID   Q47S43_THEFY            Unreviewed;       429 AA.
AC   Q47S43;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   07-JUN-2017, entry version 73.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:AAZ54724.1};
DE            EC=2.6.1.- {ECO:0000313|EMBL:AAZ54724.1};
GN   OrderedLocusNames=Tfu_0686 {ECO:0000313|EMBL:AAZ54724.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54724.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP000088; AAZ54724.1; -; Genomic_DNA.
DR   RefSeq; WP_011291133.1; NC_007333.1.
DR   ProteinModelPortal; Q47S43; -.
DR   STRING; 269800.Tfu_0686; -.
DR   EnsemblBacteria; AAZ54724; AAZ54724; Tfu_0686.
DR   KEGG; tfu:Tfu_0686; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K00823; -.
DR   OMA; HSSTLYL; -.
DR   OrthoDB; POG091H0ER2; -.
DR   BioCyc; TFUS269800:GI42-701-MONOMER; -.
DR   Proteomes; UP000000434; 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:AAZ54724.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Transferase {ECO:0000313|EMBL:AAZ54724.1}.
SQ   SEQUENCE   429 AA;  45602 MW;  7BA5EC444F19E85D CRC64;
     MSDLLARHRA VMPAWMPLYY ETPIEIVSGK GNRVVDADGN TYLDFFAGIV TNMIGYDVAE
     VREAVEAQLA RGVVHTSTLY LLRGQVELAE KIARLSGIPD AKVFFTNSGT EANETALLLA
     TYARRSDEVL ALRNSYHGRS YGTIAVTGNR GWKNSSLSPL TVHYLHGTDR SHPAFAHLSD
     REYIDVCVAD LRDVLSTTAP NVACLIAEPI QGVGGFVMPP DGLFAAYKEV LDEQGILFIS
     DEVQTGWGRT GTSFWGIGNH GVTPDMMTFA KGLGNGFAIG GVVARGDLMD ALPANGVSTF
     GGNPISTAAA NATLDYVLDH DLQANAARLG PLVLERLQPL EQLPTVSAVR GRGLMFAIDM
     ADPATGAPSA ELAVAVLEET RKRGLLIGKG GLHGQTLRMA PPLTLTEEEA EEGAAILVDA
     VTAVNDAVA
//
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