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Database: UniProt/TrEMBL
Entry: A0A0D6ACJ5_9CHRO
LinkDB: A0A0D6ACJ5_9CHRO
Original site: A0A0D6ACJ5_9CHRO 
ID   A0A0D6ACJ5_9CHRO        Unreviewed;       420 AA.
AC   A0A0D6ACJ5;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   25-OCT-2017, entry version 15.
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=GM3708_894 {ECO:0000313|EMBL:BAQ60488.1};
OS   Geminocystis sp. NIES-3708.
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Chroococcaceae; Geminocystis.
OX   NCBI_TaxID=1615909 {ECO:0000313|EMBL:BAQ60488.1, ECO:0000313|Proteomes:UP000060542};
RN   [1] {ECO:0000313|EMBL:BAQ60488.1, ECO:0000313|Proteomes:UP000060542}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-3708 {ECO:0000313|EMBL:BAQ60488.1,
RC   ECO:0000313|Proteomes:UP000060542};
RA   Hirose Y.;
RT   "Geminocystis sp. NIES-3708 complete genome sequence.";
RL   Submitted (MAR-2015) 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; AP014815; BAQ60488.1; -; Genomic_DNA.
DR   RefSeq; WP_066344417.1; NZ_AP014815.1.
DR   EnsemblBacteria; BAQ60488; BAQ60488; GM3708_894.
DR   KEGG; gee:GM3708_894; -.
DR   PATRIC; fig|1615909.3.peg.914; -.
DR   KO; K00627; -.
DR   Proteomes; UP000060542; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000060542};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00100674};
KW   Pyruvate {ECO:0000313|EMBL:BAQ60488.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000060542};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:BAQ60488.1}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   COILED       69     96       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   420 AA;  44560 MW;  94A0FB125971E662 CRC64;
     MIHDIFMPAL SSTMTEGKIV SWEKAPGDKI EKGETVVVVE SDKADMDVES FYSGYLATIL
     VPAGEEAPVG QAIAYIAETE AEIEEAKQKA SQGQQATPAP QNEVKAEPDP IVTATVNTTA
     KTNGRIVVSP RAKKLAKEFK VDLSNIVGTG LNGRIIAEDV EKLAGKVPQT PKVSPVIATV
     TATPSIAPAP IPVNNLAGQT IPFNTLQQAV IRNMMASLQV PTFQVSYSIN TDQLDSLYRK
     IKSKGVTMTA LLAKAVAVTL QKHPVVNASF SEAGIKYNES INIAVAVAMP DGGLITPVIK
     NADQIDIYSL ARNWQDLVNR ARAKQLQPDE YTTGTFTLSN LGMFGVSNFT AILPPGLGSI
     LAIGGASPTV VANGDGLFGV KNQMSVNITC DHRIIYGADA AAFLQDLAKL IETDVQSLTL
//
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