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Database: UniProt/TrEMBL
Entry: Q3AZ47_SYNS9
LinkDB: Q3AZ47_SYNS9
Original site: Q3AZ47_SYNS9 
ID   Q3AZ47_SYNS9            Unreviewed;       448 AA.
AC   Q3AZ47;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   25-OCT-2017, entry version 85.
DE   RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE            EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN   OrderedLocusNames=Syncc9902_0662 {ECO:0000313|EMBL:ABB25630.1};
OS   Synechococcus sp. (strain CC9902).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316279 {ECO:0000313|EMBL:ABB25630.1, ECO:0000313|Proteomes:UP000002712};
RN   [1] {ECO:0000313|Proteomes:UP000002712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9902 {ECO:0000313|Proteomes:UP000002712};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Synechococcus sp. CC9902.";
RL   Submitted (AUG-2005) 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; CP000097; ABB25630.1; -; Genomic_DNA.
DR   RefSeq; WP_011359474.1; NC_007513.1.
DR   ProteinModelPortal; Q3AZ47; -.
DR   STRING; 316279.Syncc9902_0662; -.
DR   EnsemblBacteria; ABB25630; ABB25630; Syncc9902_0662.
DR   KEGG; sye:Syncc9902_0662; -.
DR   eggNOG; ENOG4107UKP; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281566; -.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; POG091H04EL; -.
DR   BioCyc; SSP316279:GJCI-672-MONOMER; -.
DR   Proteomes; UP000002712; 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:UP000002712};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Pyruvate {ECO:0000313|EMBL:ABB25630.1};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:ABB25630.1}.
FT   DOMAIN        3     81       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   448 AA;  45898 MW;  BF343028A4DC276B CRC64;
     MATHDIFMPA LSSTMTEGKI VEWLKQPGDK VARGESVLVV ESDKADMDVE SFQDGFLAAV
     LMPAGSTAPV GETIGLIVET EAEIADAKAN APAAPAAAAA PAPTPTPAPT PAAVQASTTS
     PAPAPAAPPV VTAPPVVTAP VVNDGRIVAS PRAKKLASQM GVDLSTVRGS GPHGRIQAED
     VEQATGQPIS VPRVAEGTAP AAGGSVTSAA APAAAAPAGN SFGRPGETVA FNTLQGAVNR
     NMEASLAVPC FRVGYTITTD KLDAFYKKVK PKGVTMTALL AKAVAVTLAH HPQVNAATTA
     AGMSYPADVN VAVAVAMEDG GLITPVLRQA DRTDLYEMSR QWADLVKRSR SKQLLPEEYS
     TGTFTLSNLG MFGVDRFDAI LPPGTGAILA VAASRPMVVA GKDGSISVKR QMQVNLTADH
     RVVYGADGAS FLKALADLIE NRPESLAL
//
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