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Database: UniProt/TrEMBL
Entry: D1AAX5_THECD
LinkDB: D1AAX5_THECD
Original site: D1AAX5_THECD 
ID   D1AAX5_THECD            Unreviewed;       431 AA.
AC   D1AAX5;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   07-JUN-2017, entry version 48.
DE   SubName: Full=Aminotransferase class-III {ECO:0000313|EMBL:ACY98918.1};
GN   OrderedLocusNames=Tcur_3380 {ECO:0000313|EMBL:ACY98918.1};
OS   Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 /
OS   NBRC 15933 / NCIMB 10081 / Henssen B9).
OC   Bacteria; Actinobacteria; Streptosporangiales; Thermomonosporaceae;
OC   Thermomonospora.
OX   NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY98918.1, ECO:0000313|Proteomes:UP000001918};
RN   [1] {ECO:0000313|EMBL:ACY98918.1, ECO:0000313|Proteomes:UP000001918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 /
RC   Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX   PubMed=21475583; DOI=10.4056/sigs.1453580;
RA   Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S.,
RA   Del Rio T.G., Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A.,
RA   Chen A., Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Han C., Detter J.C., Rohde M., Goker M.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Thermomonospora curvata type strain
RT   (B9).";
RL   Stand. Genomic Sci. 1:13-22(2011).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP001738; ACY98918.1; -; Genomic_DNA.
DR   RefSeq; WP_012853702.1; NC_013510.1.
DR   ProteinModelPortal; D1AAX5; -.
DR   STRING; 471852.Tcur_3380; -.
DR   EnsemblBacteria; ACY98918; ACY98918; Tcur_3380.
DR   KEGG; tcu:Tcur_3380; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K00823; -.
DR   OMA; HSSTLYL; -.
DR   OrthoDB; POG091H0APS; -.
DR   BioCyc; TCUR471852:GHHD-3366-MONOMER; -.
DR   Proteomes; UP000001918; 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:ACY98918.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001918};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001918};
KW   Transferase {ECO:0000313|EMBL:ACY98918.1}.
SQ   SEQUENCE   431 AA;  45902 MW;  157F70E009F27F27 CRC64;
     MSDLLARHRA VMPNWMALYY ERPIEIVSGK GVRVTDAEGN TYLDFFAGII TNILGYDVEE
     VRQAVERQLA TGVVHTSTAY LLRGQVELAE KIVALSGIKD AKVFFVNSGT EANETALLLA
     TYARKSNQVL AMRQSYHGRS FGAIGVTANR SWKNNAYTPL TVHFLHGGDR HLPQFAHLSD
     ADFIKVCTED LRHVLATATG GDVAALIAEP IQGVGGFTMP PDGLYAAYKE VLDEYGALFI
     SDEVQTGWGR TGQSFFGIHN HGVTPDIMTF AKGLGNGFAV GGVVARGDLM DAPHATGLST
     FGGNPIAMAA ANATLDYILD HDLQSNAARQ GALLLDGLKE AAPRLPVVGA VRGKGLMFAV
     ELVEPGTGEP SPPLAAAVME ETRKRGLLVG KGGLYGNVIR MAPPLTITEE DAREGLGILI
     DSLEAVSEAA K
//
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