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Database: UniProt/TrEMBL
Entry: A0A0X8WVA7_9CYAN
LinkDB: A0A0X8WVA7_9CYAN
Original site: A0A0X8WVA7_9CYAN 
ID   A0A0X8WVA7_9CYAN        Unreviewed;       438 AA.
AC   A0A0X8WVA7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   20-DEC-2017, entry version 13.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   Name=pdhC {ECO:0000313|EMBL:BAU42345.1};
GN   ORFNames=O77CONTIG1_02166 {ECO:0000313|EMBL:BAU42345.1};
OS   Leptolyngbya sp. O-77.
OC   Bacteria; Cyanobacteria; Synechococcales; Leptolyngbyaceae;
OC   Leptolyngbya.
OX   NCBI_TaxID=1080068 {ECO:0000313|EMBL:BAU42345.1, ECO:0000313|Proteomes:UP000057790};
RN   [1] {ECO:0000313|EMBL:BAU42345.1, ECO:0000313|Proteomes:UP000057790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O-77 {ECO:0000313|EMBL:BAU42345.1,
RC   ECO:0000313|Proteomes:UP000057790};
RA   Tran K.T., Nguyen T.N., Yoon K-S., Ogo S.;
RT   "Complete genome sequence of Leptolyngbya sp. O-77.";
RL   Submitted (JAN-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; AP017367; BAU42345.1; -; Genomic_DNA.
DR   RefSeq; WP_068510321.1; NZ_AP017367.1.
DR   EnsemblBacteria; BAU42345; BAU42345; O77CONTIG1_02166.
DR   KEGG; let:O77CONTIG1_02166; -.
DR   PATRIC; fig|1080068.3.peg.2467; -.
DR   KO; K00627; -.
DR   Proteomes; UP000057790; 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; 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;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:BAU42345.1}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000057790};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Pyruvate {ECO:0000313|EMBL:BAU42345.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000057790};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:BAU42345.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      132    169       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   COILED       69     89       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   438 AA;  45341 MW;  BE93AD46264836F0 CRC64;
     MIHEVFMPAL SSTMTEGKIV SWVKAPGDKI EKGETVVVVE SDKADMDVES FYEGYLATII
     VDAGSTAPVG EAIALIAETE AEIEAAKQKA ASASAPAPAA PTPAPATTEP EPVAATVEEA
     IASSNGSSGR LVVSPRARKL AKELKVDLAT LKGSGPHGRI VAEDVEAAVG KVSEPATAAV
     TPAAAAVAAP VTAPAPAPAP ATPKPAPAPA APVTPGQVVP LTTLQNAVVR NMVASLEVPT
     FHVGYTITTD NLDKLYKQIK SKGVTMTALL AKAVAVTLKK HPLLYAAYTD QGIKYNSGIN
     VAVAVAMDDG GLITPVLQAA DQMDIYTLSR TWKDLVDRAR SKQLQPAEYS TGTFTLSNLG
     MFGVDRFDAI LPPGQGAILA IGASRPQVVA TAEGLFGVRT QMQVNLTADH RIIYGAHAAA
     FLQDLAKLIE TDAQSLTL
//
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