(data stored in ACNUC7421 zone)

SWISSPROT: Q47TH0_THEFY

ID   Q47TH0_THEFY            Unreviewed;       431 AA.
AC   Q47TH0;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 84.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:AAZ54244.1};
DE            EC=2.6.1.- {ECO:0000313|EMBL:AAZ54244.1};
GN   OrderedLocusNames=Tfu_0206 {ECO:0000313|EMBL:AAZ54244.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54244.1, 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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000088; AAZ54244.1; -; Genomic_DNA.
DR   RefSeq; WP_011290653.1; NC_007333.1.
DR   STRING; 269800.Tfu_0206; -.
DR   EnsemblBacteria; AAZ54244; AAZ54244; Tfu_0206.
DR   KEGG; tfu:Tfu_0206; -.
DR   eggNOG; ENOG41088V7; Bacteria.
DR   eggNOG; COG0161; LUCA.
DR   HOGENOM; HOG000221644; -.
DR   OMA; MKLARHY; -.
DR   OrthoDB; 478143at2; -.
DR   BioCyc; TFUS269800:G1G4Q-210-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; -; 1.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47TH0.
DR   SWISS-2DPAGE; Q47TH0.
KW   Aminotransferase {ECO:0000313|EMBL:AAZ54244.1};
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:AAZ54244.1}.
SQ   SEQUENCE   431 AA;  45472 MW;  726DD53A354B174C CRC64;
     MSHTTSTALW PYLLPPSAHG DDSICAVSAR GHRVRFADGR ELLCGASGLW NANLGYGNPA
     IAQAVAQALH DASYLSAFRY ENVYARRAAA DLIEVSGPEH YSRVLFSSSG GAANDAAMKV
     ARHYHALLGR TRRSLVVSLR GSYHGLTFGG FALTGEDLGQ RLYGVDQRLV RHVRPNDTAE
     LNALVSRAAK QIAAVVVEPV VGTGTIPLTD EYVAELLRLR AEHGFLLIAD EVATGFGRTG
     SFFASQRWPE QPDLLITSKG LTNGTCPASA VIVSQRVADA FTEHDAVLSH AETQGATPLT
     CAAISATIAE MRRLDAVAAG QALGEKLGAG IAELMAEMPQ IIGTTGVGCF RSLRIADASG
     APLPQHRVPA LVAAIRDAGA IVHPGPSGVQ LVPALTYSDA ELAELLDCVR RGILLMSSLS
     APGGRWLRGC R
//

If you have problems or comments...

PBIL Back to PBIL home page