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Database: UniProt/TrEMBL
Entry: K9SRK8_9SYNE
LinkDB: K9SRK8_9SYNE
Original site: K9SRK8_9SYNE 
ID   K9SRK8_9SYNE            Unreviewed;       430 AA.
AC   K9SRK8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   07-JUN-2017, entry version 26.
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=Syn7502_00631 {ECO:0000313|EMBL:AFY72780.1};
OS   Synechococcus sp. PCC 7502.
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=1173263 {ECO:0000313|EMBL:AFY72780.1, ECO:0000313|Proteomes:UP000010385};
RN   [1] {ECO:0000313|EMBL:AFY72780.1, ECO:0000313|Proteomes:UP000010385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7502 {ECO:0000313|EMBL:AFY72780.1,
RC   ECO:0000313|Proteomes:UP000010385};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y.,
RA   Chain P., Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA   Ivanova N., Mikhailova N., Ovchinnikova G., Pagani I., Pati A.,
RA   Goodwin L., Peters L., Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Synechococcus sp. PCC 7502.";
RL   Submitted (MAY-2012) 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; CP003594; AFY72780.1; -; Genomic_DNA.
DR   RefSeq; WP_015167439.1; NC_019702.1.
DR   EnsemblBacteria; AFY72780; AFY72780; Syn7502_00631.
DR   KEGG; synp:Syn7502_00631; -.
DR   PATRIC; fig|1173263.3.peg.648; -.
DR   KO; K00627; -.
DR   OrthoDB; POG091H04EL; -.
DR   BioCyc; SSP1173263:GLM0-610-MONOMER; -.
DR   Proteomes; UP000010385; 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; 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:AFY72780.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010385};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Pyruvate {ECO:0000313|EMBL:AFY72780.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010385};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:AFY72780.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   430 AA;  45509 MW;  D1D8336FCED346A9 CRC64;
     MIYEIFMPAL SSTMTEGKIT AWVKSIGDKV EKGETVLVVE SDKADMDVES FYEGYLGAIA
     VPAGETAPVG STLGYVAETV AEIADIKSKL SQTSEPVAAS TNGTSTGTAI PEVVVTKVET
     PAIAKSDRLI ATPRAKRIAK ENNLDLAKIN GSGPNGRITE QDVTALLQVP VQATPAKVSV
     KAPEPIAASI PSAPVSTTPK VTYTPQLGTT KPLTTLQNAV VRNMNASLSV PTFHVGYTIT
     TTGLDELYKQ IKSKGVTITA LLAKAVAVTL QRHPIVNASF SDQGIVYKSD INVAIAVAME
     DGGLITPVLP KANESDIYSL SRHWKSLVER ARAKQLQPEE YNSGTFTISN LGMFGVDRFD
     AILPPNTGAI LAIGASHPQV VATKDGAIAV RNQMQVNLTA DHRIIYGADA AKFLQDLAKL
     LETDAQSLVL
//
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