(data stored in ACNUC7421 zone)

SWISSPROT: Q47TJ4_THEFY

ID   Q47TJ4_THEFY            Unreviewed;       446 AA.
AC   Q47TJ4;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 97.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   OrderedLocusNames=Tfu_0182 {ECO:0000313|EMBL:AAZ54220.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54220.1, 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   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU003423};
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003423}.
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DR   EMBL; CP000088; AAZ54220.1; -; Genomic_DNA.
DR   RefSeq; WP_011290629.1; NC_007333.1.
DR   STRING; 269800.Tfu_0182; -.
DR   EnsemblBacteria; AAZ54220; AAZ54220; Tfu_0182.
DR   KEGG; tfu:Tfu_0182; -.
DR   eggNOG; ENOG4107RN0; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281564; -.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; 1626282at2; -.
DR   BioCyc; TFUS269800:G1G4Q-185-MONOMER; -.
DR   Proteomes; UP000000434; Chromosome.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q47TJ4.
DR   SWISS-2DPAGE; Q47TJ4.
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:AAZ54220.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:AAZ54220.1}.
FT   DOMAIN        6     81       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      146    183       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   446 AA;  47709 MW;  7BA742364773623C CRC64;
     MTHQGIQQFV LPDVGEGLTE AEILTWHVQP GDQVDVNQVI CEIETAKAVV ELPSPFAGRV
     EALLVEAGET VPVGTPIIAV DTGGAAGEPR PEPAPAAAPA EPPAEEKREP VLVGYGVKSG
     ATKRRARRRT PSAVPAQTVG QRTVVLAKPP VRKLAKDLGV DLRTVVPSGP NGVITRDDVR
     RHAEQNQPQP SAPRVPEPAA PAPAASPAPE RDVREERIPV KGVLKHMAAA MVDSAFTAPH
     VTEFLQVDVT KTVKVVQKLR QRPEFADVKV SPLLLVARAL LIAVRRHPRI NASWDEANQE
     VVVKHYVNLG IAAATDRGLV VPNIKEADRL PLPDLARALT DLTEKARAGQ TAPADLTGGT
     ITITNIGVFG IDGGTPILNR GEAAILALGQ IRDMPWVHKG KIKIRKVTTL SLSFDHRLVD
     GELGSKVLRD VATILEDPEE MVLAWG
//

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