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Database: UniProt/TrEMBL
Entry: A5GJ93_SYNPW
LinkDB: A5GJ93_SYNPW
Original site: A5GJ93_SYNPW 
ID   A5GJ93_SYNPW            Unreviewed;       449 AA.
AC   A5GJ93;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   28-MAR-2018, entry version 67.
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:CAK23008.1};
GN   OrderedLocusNames=SynWH7803_0582 {ECO:0000313|EMBL:CAK23008.1};
OS   Synechococcus sp. (strain WH7803).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=32051 {ECO:0000313|EMBL:CAK23008.1, ECO:0000313|Proteomes:UP000001566};
RN   [1] {ECO:0000313|Proteomes:UP000001566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH7803 {ECO:0000313|Proteomes:UP000001566};
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; CT971583; CAK23008.1; -; Genomic_DNA.
DR   ProteinModelPortal; A5GJ93; -.
DR   STRING; 32051.SynWH7803_0582; -.
DR   EnsemblBacteria; CAK23008; CAK23008; SynWH7803_0582.
DR   KEGG; syx:SynWH7803_0582; -.
DR   eggNOG; ENOG4107UKP; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281566; -.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; POG091H04EL; -.
DR   Proteomes; UP000001566; 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; 3.30.559.10; -; 1.
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; IPR023213; CAT-like_dom_sf.
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:CAK23008.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001566};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Pyruvate {ECO:0000313|EMBL:CAK23008.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001566};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:CAK23008.1}.
FT   DOMAIN        3     78       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      151    188       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   449 AA;  45880 MW;  76CE7DE2F742EADA CRC64;
     MATHDIFMPA LSSTMTEGKI VEWLKKPGDK VARGESVLVV ESDKADMDVE SFNDGFLASV
     LMPAGSTAPV GETIGLIVES EAEIAEAQAK APSGGAAAPA SAPAAAAAPP AAPSAPTPVP
     SAPVSSPPPA TAPPAPAAVP APAPTGTGRL IVSPRAKKLA AQMGVDLSSL RGSGPNGRIQ
     AEDVERAAGR PVSVPQVGEG TAPAALAGGA VPAPPSAPAG NSFGRPGETV PFNTLQAAVN
     RNMEASLAVP SFRVGYTITT DKLDAFYKQV KPKGVTMTAL LAKAVAVTLA RHPQVNAATT
     QAGMAYPADV NVAVAVAMED GGLITPVLRQ ADRIDLYELS RQWGDLVKRS RSKQLQPEEY
     STGTFTLSNL GMFGVDRFDA ILPPGTGAIL AVAASRPTVV AAKDGSIAVK RQMQVNLTAD
     HRVIYGADGA AFLKDLAELI EMRPESLAL
//
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