(data stored in ACNUC7421 zone)

SWISSPROT: Q47TA1_THEFY

ID   Q47TA1_THEFY            Unreviewed;       462 AA.
AC   Q47TA1;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 86.
DE   SubName: Full=Aminotransferase {ECO:0000313|EMBL:AAZ54316.1};
DE            EC=2.6.1.- {ECO:0000313|EMBL:AAZ54316.1};
GN   OrderedLocusNames=Tfu_0278 {ECO:0000313|EMBL:AAZ54316.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54316.1, 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; AAZ54316.1; -; Genomic_DNA.
DR   STRING; 269800.Tfu_0278; -.
DR   EnsemblBacteria; AAZ54316; AAZ54316; Tfu_0278.
DR   KEGG; tfu:Tfu_0278; -.
DR   eggNOG; ENOG4108JPX; Bacteria.
DR   eggNOG; COG0161; LUCA.
DR   HOGENOM; HOG000020207; -.
DR   OMA; AHKVPNT; -.
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; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47TA1.
DR   SWISS-2DPAGE; Q47TA1.
KW   Aminotransferase {ECO:0000313|EMBL:AAZ54316.1};
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:AAZ54316.1}.
SQ   SEQUENCE   462 AA;  50843 MW;  2A769542436E4C33 CRC64;
     MTVRSGSGLA ANDFQQAAKD HLWMHFTELA AYQDTDVPVI TRGEGPYVYD TNGKRYLDGL
     AGLFVSQVGH GRTEIAEAIA EQSRKLAYFP IWTYAHPTAI ELADRLADLA PGDLNRVFFT
     TSGSEAVESA WKLARQYFKL IGQPTRHKVI SRRIAYHGTT MGALSITGLQ AIKTPFEPLV
     PSTIQVPNTN IYRAPVHGDD PEAFGRWAAD QVEEAILQND PESIAAVYVE PVQNSGGCFP
     PPPGYFQRLR EICDRYGVLL VSDEVICAFG RVGAYFGAQR FDYLPDIITF AKGVTSGYVP
     MGGLIAREHL VEPFREAGNT FLHGSTFAGH PVAAAAALAN LDIFEREGLI DHVQANAPAF
     RATLEKLLDL PIVGDVRGEG YFYGIELVKD KETKETFTDE EAHRLLKGFL SPALFDAGLV
     CRADDRGEPV VQLSPPLICG PEHFAEMESI LREVLTEAWQ RI
//

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