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Database: UniProt/TrEMBL
Entry: A0A076H340_9SYNE
LinkDB: A0A076H340_9SYNE
Original site: A0A076H340_9SYNE 
ID   A0A076H340_9SYNE        Unreviewed;       446 AA.
AC   A0A076H340;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   25-OCT-2017, entry version 17.
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=KR100_12475 {ECO:0000313|EMBL:AII44165.1};
OS   Synechococcus sp. KORDI-100.
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1280380 {ECO:0000313|EMBL:AII44165.1, ECO:0000313|Proteomes:UP000028591};
RN   [1] {ECO:0000313|EMBL:AII44165.1, ECO:0000313|Proteomes:UP000028591}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KORDI-100 {ECO:0000313|EMBL:AII44165.1,
RC   ECO:0000313|Proteomes:UP000028591};
RA   Choi D.H., Kwon K.-K., Lee J.-H., Noh J.H.;
RT   "Genome sequence of Synechococcus sp. KORDI-100.";
RL   Submitted (JUN-2013) 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; CP006269; AII44165.1; -; Genomic_DNA.
DR   RefSeq; WP_038546041.1; NZ_CP006269.1.
DR   EnsemblBacteria; AII44165; AII44165; KR100_12475.
DR   KEGG; synk:KR100_12475; -.
DR   KO; K00627; -.
DR   Proteomes; UP000028591; 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:UP000028591};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028591};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN        3     81       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   446 AA;  45826 MW;  355AC41AB8D1EEF1 CRC64;
     MATFDIFMPA LSSTMTEGKI VEWLKQPGDK VGRGESVLVV ESDKADMDVE SFQDGFLAAV
     LMPAGSTAPV GETIGLIVET EAEIAEAKAK APTSSAPVSA AVEAQPAPAA PAAPAPVVAA
     PAATPAPAPA PPAPAPAAPV VNDGRIVASP RARKLASQMG VDLATVRGSG PHGRIQADDV
     ERASGQPISV PRVAEGSAPA ANGQGAAAPA AAAAPAGNSF GRPGETVAFN TLQGAVNRNM
     EASLAVPCFR VGYTITTDKL DRFYKQVKPK GVTMTALLAK AVAVTLARHP QVNAATTPAG
     MAYPAEVNVA VAVAMEDGGL ITPVLRQADR TDLYEMSRQW KDLVKRSRSK QLQPEEYSTG
     TFTLSNLGMF GVDRFDAILP PGTGAILAVA ASRSTVVAGA DGSIAVKRQM QVNLTADHRV
     IYGADGAAFL KDLAELIELR PESLAL
//
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