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Database: UniProt/TrEMBL
Entry: B7K3F5_CYAP8
LinkDB: B7K3F5_CYAP8
Original site: B7K3F5_CYAP8 
ID   B7K3F5_CYAP8            Unreviewed;       426 AA.
AC   B7K3F5;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   25-OCT-2017, entry version 62.
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=PCC8801_1231 {ECO:0000313|EMBL:ACK65297.1};
OS   Cyanothece sp. (strain PCC 8801) (Synechococcus sp. (strain PCC 8801 /
OS   RF-1)).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Oscillatoriales;
OC   Cyanothecaceae; Cyanothece.
OX   NCBI_TaxID=41431 {ECO:0000313|EMBL:ACK65297.1, ECO:0000313|Proteomes:UP000008204};
RN   [1] {ECO:0000313|Proteomes:UP000008204}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 8801 {ECO:0000313|Proteomes:UP000008204};
RX   PubMed=21972240; DOI=10.1128/mBio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M.,
RA   Min H., Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a
RT   group of unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
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; CP001287; ACK65297.1; -; Genomic_DNA.
DR   RefSeq; WP_012594571.1; NC_011726.1.
DR   ProteinModelPortal; B7K3F5; -.
DR   STRING; 41431.PCC8801_1231; -.
DR   EnsemblBacteria; ACK65297; ACK65297; PCC8801_1231.
DR   KEGG; cyp:PCC8801_1231; -.
DR   eggNOG; ENOG4107UKP; Bacteria.
DR   eggNOG; COG0508; LUCA.
DR   HOGENOM; HOG000281566; -.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; POG091H04EL; -.
DR   Proteomes; UP000008204; 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:UP000008204};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008204};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   426 AA;  44933 MW;  88848F34B8E0FA03 CRC64;
     MIHDIFMPAL SSTMTEGKIV SWVKSPGDKV AKGETVVVVE SDKADMDVES FYEGYLATIL
     VEAGQEAPVG TAIALIAETE AEITQAQQQQ KPPSATAEPS RETTSPPVAS PQPVPTVTAT
     PTVTASNGNG RTVASPRAKK LAKELGVDLK TLRGSGPYGR IVAGDVERAT SKVTTVTPTL
     TPTPTVQPTP TPSTPPTPVP ATPGETVPLT TLQKAVVQNM VATVQVPTYH VGYTITTDAL
     DKLYKQLKSK GVTMTALLAK AVAMAVQKHP LVNASYTDQG IKYNGSINVA LAVAMDDGGL
     ITPVLQNADQ VDIYSLSRTW KDLVDRARSK QLQPQEYNSG TITVSNLGMF GVDRFDAILP
     PGQGAILAIG ASRPQVVATP DGLIGVQRQM AVNITCDHRV IYGAHAAAFL QDLAKVIETD
     VQSLTM
//
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