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Database: UniProt/TrEMBL
Entry: A0A1D8TMW8_9CYAN
LinkDB: A0A1D8TMW8_9CYAN
Original site: A0A1D8TMW8_9CYAN 
ID   A0A1D8TMW8_9CYAN        Unreviewed;       436 AA.
AC   A0A1D8TMW8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   25-OCT-2017, entry version 7.
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=BJP34_05370 {ECO:0000313|EMBL:AOW98954.1};
OS   Moorea producens PAL-8-15-08-1.
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Oscillatoriaceae; Moorea.
OX   NCBI_TaxID=1458985 {ECO:0000313|EMBL:AOW98954.1, ECO:0000313|Proteomes:UP000177870};
RN   [1] {ECO:0000313|EMBL:AOW98954.1, ECO:0000313|Proteomes:UP000177870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAL-8-15-08-1 {ECO:0000313|EMBL:AOW98954.1,
RC   ECO:0000313|Proteomes:UP000177870};
RA   Leao T., Castelao G., Korobeynikov A., Monroe E.A., Podell S.,
RA   Glukhov E., Allen E., Gerwick W.H., Gerwick L.;
RT   "Comparative genomics uncovers the prolific and rare metabolic
RT   potential of the cyanobacterial genus Moorea.";
RL   Submitted (OCT-2016) 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; CP017599; AOW98954.1; -; Genomic_DNA.
DR   RefSeq; WP_070391456.1; NZ_CP017599.1.
DR   KEGG; mpro:BJP34_05370; -.
DR   KO; K00627; -.
DR   Proteomes; UP000177870; 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:UP000177870};
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   436 AA;  46150 MW;  3DC9624FBFFB1B51 CRC64;
     MIHEVFMPAL SSTMTEGKIV SWEKSPGDKV EKGETVVVVE SDKADMDVES FYEGYLATIT
     VSAGDSAPVG APIALIAETE AEIEAAKQQA AQSTPATDTA TPQQATASTP EPVQTALAAV
     ADTPSRRNGR IIASPRARKL AKELRVDLNT LRGSGPHGRI VAEDVEAAAG KGSTPPAPAT
     TTPAPLPTAA VMPTPTPATM PAPLPAPPAA VPLGEVVPFN TLQNAVVRNM MVSLQVPTFR
     VGYTITTDEL DKLYKKIKPK GVTMTGLLAK AVAVTLQKHP LVNASYTERG IQYHSSINVA
     VAVAMADGGL ITPVLRHAEQ LDIYSLSRTW KDLVDRARTK QLQPEEYNSG TFTLSNLGMF
     GVDRFDAILP PGQGSILAIG ASRPTVVATP DGMMGVKRQM QVNITCDHRI IYGTDAAAFL
     QDLAKLIETD PQSLTL
//
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