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Database: UniProt/TrEMBL
Entry: A5GUY8_SYNR3
LinkDB: A5GUY8_SYNR3
Original site: A5GUY8_SYNR3 
ID   A5GUY8_SYNR3            Unreviewed;       444 AA.
AC   A5GUY8;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   25-OCT-2017, entry version 66.
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:CAK28697.1};
GN   OrderedLocusNames=SynRCC307_1794 {ECO:0000313|EMBL:CAK28697.1};
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278 {ECO:0000313|EMBL:CAK28697.1, ECO:0000313|Proteomes:UP000001115};
RN   [1] {ECO:0000313|Proteomes:UP000001115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307 {ECO:0000313|Proteomes:UP000001115};
RG   Genoscope;
RL   Submitted (MAY-2006) 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; CT978603; CAK28697.1; -; Genomic_DNA.
DR   RefSeq; WP_011936210.1; NC_009482.1.
DR   ProteinModelPortal; A5GUY8; -.
DR   STRING; 316278.SynRCC307_1794; -.
DR   EnsemblBacteria; CAK28697; CAK28697; SynRCC307_1794.
DR   KEGG; syr:SynRCC307_1794; -.
DR   eggNOG; ENOG4107UKP; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281566; -.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; POG091H04EL; -.
DR   Proteomes; UP000001115; 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   ECO:0000313|EMBL:CAK28697.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001115};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Pyruvate {ECO:0000313|EMBL:CAK28697.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001115};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:CAK28697.1}.
FT   DOMAIN        3     78       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   444 AA;  45002 MW;  BB07D55E74E4CFF8 CRC64;
     MATFEIFMPA LSSTMTEGKI VEWLKQPGDR VERGESVLVV ESDKADMDVE SFEAGFLGAV
     LLPAGGTAPV GETIGLVVET EAELAELKAN GPAKPAASAP AAAPAPAPAA APPAAPEPAP
     APTPAPVAVA APPAPASSNG HGGRVVASPR AKKLAQQLGV QLEGLRGSGP HGRLIAADIE
     RAAGRTPTAP AAVPAGTLTA AQAAAPAVAP LPAAVAAPVA PGETLPFTTL QQAVNRNMVA
     SLAVPTFRVG YTITTDKLDA FYKQVKPKGV TMTALLAKAV ASALAGHPRV NAAFSEAGIA
     YPEGINVAVA VAMEDGGLVT PVLAAADRND LYSLSRSWAD LVSRARSKQL KPEEYSTGTF
     TLSNLGMFGV DRFDAILPPG TGAILAVGAS RPVVAANSDG SIAVKRQMQV NLTADHRVIY
     GADAAGFLKD LAKIIETQPE SLAL
//
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