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Database: UniProt/TrEMBL
Entry: A0A0S3U9N3_9CYAN
LinkDB: A0A0S3U9N3_9CYAN
Original site: A0A0S3U9N3_9CYAN 
ID   A0A0S3U9N3_9CYAN        Unreviewed;       427 AA.
AC   A0A0S3U9N3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   25-OCT-2017, entry version 12.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   ORFNames=LEP3755_47980 {ECO:0000313|EMBL:BAU14252.1};
OS   Leptolyngbya sp. NIES-3755.
OC   Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae;
OC   Leptolyngbya.
OX   NCBI_TaxID=1752064 {ECO:0000313|EMBL:BAU14252.1};
RN   [1] {ECO:0000313|EMBL:BAU14252.1, ECO:0000313|Proteomes:UP000062150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-3755 {ECO:0000313|EMBL:BAU14252.1,
RC   ECO:0000313|Proteomes:UP000062150};
RA   Hirose Y.;
RT   "Complete genome sequence of Leptolyngbya sp. NIES-3755.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
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; AP017308; BAU14252.1; -; Genomic_DNA.
DR   RefSeq; WP_068388678.1; NZ_AP017308.1.
DR   EnsemblBacteria; BAU14252; BAU14252; LEP3755_47980.
DR   KEGG; len:LEP3755_47980; -.
DR   PATRIC; fig|1752064.3.peg.4981; -.
DR   KO; K00627; -.
DR   Proteomes; UP000062150; Chromosome.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
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; IPR004167; E3-bd.
DR   InterPro; IPR036625; E3-bd_dom_sf.
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.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Complete proteome {ECO:0000313|Proteomes:UP000062150};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   427 AA;  44694 MW;  CFB8F9D6240A3113 CRC64;
     MIHEIFMPAL SSTMTEGKIV SWVKSPGDKV EKGETVVVVE SDKADMDVES FYEGYLATIV
     TQAGESAPVG SAIALLAETE AEIELAKQQA ASTSAPADTP ATPAAAPEPV AVAASPNGTS
     TAPKNGRIVA SPRARKLAKD LKVELSALAG SGPHGRIVAE DVEAAAGKTV SKPPVPAAPR
     PAAPAPVAAA TSRPAAPAPT PTQPGQIQPM TTLQTAVVRN MMASLDVPVF RVGYTMTTDA
     LDKLYKQVKS KGVTMTALLA KAVAVTLQKH PLLYSSYVEN GIHFNTGINI AVAVAMEDGG
     LITPVLKNAD QQDLYSLSRN WKDLVDRARS KQLQPDEYSS GTFTISNLGM FGVDTFDAIL
     PPGQGSILAI GASRANVVAN DEGMLGVRRQ MQVNITCDHR IIYGADAAGF LRDLAKLIET
     NAQSLTL
//
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