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Database: UniProt/TrEMBL
Entry: K9YVH9_DACSA
LinkDB: K9YVH9_DACSA
Original site: K9YVH9_DACSA 
ID   K9YVH9_DACSA            Unreviewed;       429 AA.
AC   K9YVH9;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   07-JUN-2017, entry version 25.
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=Dacsa_2317 {ECO:0000313|EMBL:AFZ50931.1};
OS   Dactylococcopsis salina PCC 8305.
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Dactylococcopsis.
OX   NCBI_TaxID=13035 {ECO:0000313|EMBL:AFZ50931.1, ECO:0000313|Proteomes:UP000010482};
RN   [1] {ECO:0000313|EMBL:AFZ50931.1, ECO:0000313|Proteomes:UP000010482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 8305 {ECO:0000313|EMBL:AFZ50931.1,
RC   ECO:0000313|Proteomes:UP000010482};
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., Daligault H.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E.,
RA   Ivanova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA   Peters L., Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished genome of Dactylococcopsis salina PCC 8305.";
RL   Submitted (APR-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; CP003944; AFZ50931.1; -; Genomic_DNA.
DR   RefSeq; WP_015229923.1; NC_019780.1.
DR   EnsemblBacteria; AFZ50931; AFZ50931; Dacsa_2317.
DR   KEGG; dsl:Dacsa_2317; -.
DR   PATRIC; fig|13035.3.peg.2628; -.
DR   KO; K00627; -.
DR   OrthoDB; POG091H04EL; -.
DR   BioCyc; DSAL13035:GLCB-2165-MONOMER; -.
DR   Proteomes; UP000010482; 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:AFZ50931.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010482};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Pyruvate {ECO:0000313|EMBL:AFZ50931.1};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:AFZ50931.1}.
FT   DOMAIN        2     80       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   429 AA;  45682 MW;  98DC09F85155DE65 CRC64;
     MIRDIFMPAL SSTMTEGKIV SWAKSQGEKV EKGETVLVVE SDKADMDVES FHDGYLATIL
     VPEGEQAPVG STIGLLAETE AEIETAKQQG SNQTTATTAK TETKTETPVA PSSTPEPATP
     TPQVASTPTS TPKQENGRVV ASPRARKLAK EHNIDLATLQ GSGPHGRIVA SDVEAATGQP
     TATPQPQPTP QPAPQPTPQA APSYAKGEVV PFTTLQSSVV RNMTATVQVP TFHVGYTITT
     DALDKLYKQI KSKGVTMTAL LAKAVAATLQ KHPLVNASYS EQGIQYHSGI NIAVAVAMED
     GGLITPVLRN AAEQDIYTLS RNWKDLVKRS RSKQLQPEEY STGTFTLSNL GMFGVDRFDA
     ILPPGQGGIL AIGASRPQVV ATDDGMFGVR RQMSVNITCD HRIIYGAHAA AFLQDLAQLI
     ETDPQSLTL
//
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