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Database: UniProt/TrEMBL
Entry: K9XT52_STAC7
LinkDB: K9XT52_STAC7
Original site: K9XT52_STAC7 
ID   K9XT52_STAC7            Unreviewed;       431 AA.
AC   K9XT52;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   20-DEC-2017, entry version 30.
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=Sta7437_1277 {ECO:0000313|EMBL:AFZ34847.1};
OS   Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437).
OC   Bacteria; Cyanobacteria; Pleurocapsales; Dermocarpellaceae; Stanieria.
OX   NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ34847.1, ECO:0000313|Proteomes:UP000010473};
RN   [1] {ECO:0000313|Proteomes:UP000010473}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29371 / PCC 7437 {ECO:0000313|Proteomes:UP000010473};
RX   PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA   Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E.,
RA   Calteau A., Cai F., Tandeau de Marsac N., Rippka R., Herdman M.,
RA   Sivonen K., Coursin T., Laurent T., Goodwin L., Nolan M.,
RA   Davenport K.W., Han C.S., Rubin E.M., Eisen J.A., Woyke T., Gugger M.,
RA   Kerfeld C.A.;
RT   "Improving the coverage of the cyanobacterial phylum using diversity-
RT   driven genome sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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; CP003653; AFZ34847.1; -; Genomic_DNA.
DR   RefSeq; WP_015192520.1; NC_019748.1.
DR   EnsemblBacteria; AFZ34847; AFZ34847; Sta7437_1277.
DR   KEGG; scs:Sta7437_1277; -.
DR   PATRIC; fig|111780.3.peg.1330; -.
DR   KO; K00627; -.
DR   OMA; TMEFESF; -.
DR   OrthoDB; POG091H04EL; -.
DR   Proteomes; UP000010473; 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; 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:AFZ34847.1}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000010473};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010473};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:AFZ34847.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      133    170       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   COILED       69     96       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   431 AA;  45420 MW;  7F02B7FBD8CA2B42 CRC64;
     MIHDIFMPAL SSTMTEGKIV EWTKAPGDKV AKGETVVVVE SDKADMDVES FNEGYLAVIL
     VEAGKEAPVG NAIALLAETE AEIEEAKQKA ASLQGGSSSP AAPQSKPTPV ATPGAVADNA
     TSTTQTTSNG RIVASPRARK LAKEFGVDLK TIQGSGPYGR IVAHDIEQAA GKTPTPTSVA
     SQPVTAPVAP PPVSRPVTPS PAPVSVTPGE TVPLNTLQKA VVQNMMMSLQ VPTFHVNYTI
     TTDALDQLYK QIKSKGVTMT ALLAKAVAVT LAKHPIVNAS YSEGAIKYNS EINIAVAVAM
     EGGGLITPVL RNADKLDLYS LSRSWKDLVD RSRLKQLQPD EYSTGTFTLS NLGMFGVDRF
     DAILPPGQGS ILAVGAARPQ VVANEQGLIG VKRQMVVNMT SDHRIIYGAQ AASFLQDLAK
     LIETEPQSLT L
//
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