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Database: UniProt/TrEMBL
Entry: A0A0S3TS40_9CYAN
LinkDB: A0A0S3TS40_9CYAN
Original site: A0A0S3TS40_9CYAN 
ID   A0A0S3TS40_9CYAN        Unreviewed;       427 AA.
AC   A0A0S3TS40;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   25-OCT-2017, entry version 12.
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=FIS3754_38240 {ECO:0000313|EMBL:BAU07884.1};
OS   Fischerella sp. NIES-3754.
OC   Bacteria; Cyanobacteria; Nostocales; Hapalosiphonaceae; Fischerella.
OX   NCBI_TaxID=1752063 {ECO:0000313|EMBL:BAU07884.1};
RN   [1] {ECO:0000313|EMBL:BAU07884.1, ECO:0000313|Proteomes:UP000068400}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-3754 {ECO:0000313|EMBL:BAU07884.1,
RC   ECO:0000313|Proteomes:UP000068400};
RX   PubMed=26784989; DOI=10.1016/j.jbiotec.2016.01.011;
RA   Hirose Y., Fujisawa T., Ohtsubo Y., Katayama M., Misawa N.,
RA   Wakazuki S., Shimura Y., Nakamura Y., Kawachi M., Yoshikawa H.,
RA   Eki T., Kanesaki Y.;
RT   "Complete genome sequence of cyanobacterium Fischerella sp. NIES-3754,
RT   providing thermoresistant optogenetic tools.";
RL   J. Biotechnol. 220:45-46(2016).
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; AP017305; BAU07884.1; -; Genomic_DNA.
DR   RefSeq; WP_071846763.1; NZ_AP017305.1.
DR   EnsemblBacteria; BAU07884; BAU07884; FIS3754_38240.
DR   KEGG; fis:FIS3754_38240; -.
DR   PATRIC; fig|1752063.4.peg.4270; -.
DR   KO; K00627; -.
DR   Proteomes; UP000068400; 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:UP000068400};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN        3     78       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   427 AA;  44831 MW;  5E492C08D2AB2151 CRC64;
     MSIYEVFMPA LSSTMTEGKI VSWEKSPGDK VEKGETVVVV ESDKADMDVE SFYEGYLAHI
     IVQAGETAPV GAAIALLAET EAEIETAKSQ AQGAGTAKQE TTATAAPTKT ADTAASEKPA
     LATHNGSNHR SGRVVASPRA RKLAKELKVD LSNISGSGPY GRIVAEDVQA VIGKTSQPPA
     SAAPITPAPV VTPVATTPAV AAVPGQVVPL NTLQSAVARN MVASLSVPVI HVGYTITTDA
     LDKLYKQIKS KGVTMTALLA KAVAVTLQKH PLINANYSDQ GIVYPASINV AVAVAMDDGG
     LITPVLQNAD QLDIYSLSRT WKSLVERARV KKLQPEEYST GTFTLSNLGM FGVDRFDAIL
     PPGQGSILAI GASRPQVVAT ADGMFGIKQQ MQVNMTSDHR IIYGAHAAAF LQDLAKLIET
     NPQSLTM
//
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