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Database: UniProt/TrEMBL
Entry: A0A182ASM9_9CYAN
LinkDB: A0A182ASM9_9CYAN
Original site: A0A182ASM9_9CYAN 
ID   A0A182ASM9_9CYAN        Unreviewed;       451 AA.
AC   A0A182ASM9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   25-OCT-2017, entry version 8.
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=CBM981_2756 {ECO:0000313|EMBL:SBO44455.1};
OS   Cyanobium sp. NIES-981.
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Cyanobium.
OX   NCBI_TaxID=1851505 {ECO:0000313|EMBL:SBO44455.1, ECO:0000313|Proteomes:UP000196310};
RN   [1] {ECO:0000313|EMBL:SBO44455.1, ECO:0000313|Proteomes:UP000196310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-981 {ECO:0000313|EMBL:SBO44455.1,
RC   ECO:0000313|Proteomes:UP000196310};
RA   Lavstsen T., Jespersen J.S.;
RL   Submitted (MAY-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; LT578417; SBO44455.1; -; Genomic_DNA.
DR   KEGG; cyi:CBM981_2756; -.
DR   KO; K00627; -.
DR   Proteomes; UP000196310; Chromosome i.
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   ECO:0000313|EMBL:SBO44455.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000196310};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Pyruvate {ECO:0000313|EMBL:SBO44455.1};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:SBO44455.1}.
FT   DOMAIN        1     74       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   451 AA;  45049 MW;  4D8519642B28D182 CRC64;
     MPALSSTMTE GKIVEWLKQP GERVERGESV LVVESDKADM DVEAFQEGFL AAVLMPAGGT
     APVGETIGLI VETEEEIAAA AAAAPAAPAA ATPAPAAATP AAAAAPAAPS PVPAPAPAPV
     AAAPAPAPAA APTVTVPVSA PAPSAGGRVV ATPRAKKLAG QLGVDLGALR GSGPHGRIQA
     EDVLAATGQP ISVPRVAEGS APAAAAGGNG ASAPAPAPAG QTFGRPGEAV AFNTLQNAVN
     RNMLASLAVP TFRVGYTITT TKLDAFYKQV KSKGVTMTAL LAKAVAVTLA RHPQVNAATS
     ADGSAMAYPA AVNVAVAVAM EDGGLITPVL ASADKTDIYA LARSWADLVA RARSKQLQPE
     EYSTGTFTLS NLGMFGVDRF DAILPPGTGA ILAVAASRPC VVAGKDGSIR VANQMQVNLT
     CDHRTIYGAH AAAFLKDLAQ LIETNPESLA L
//
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