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Database: UniProt
Entry: A0A257IXM8_9BACT
LinkDB: A0A257IXM8_9BACT
Original site: A0A257IXM8_9BACT 
ID   A0A257IXM8_9BACT        Unreviewed;       421 AA.
AC   A0A257IXM8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   07-NOV-2018, entry version 5.
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=CFE22_03660 {ECO:0000313|EMBL:OYU67594.1};
OS   Cytophagaceae bacterium BCCC1.
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae.
OX   NCBI_TaxID=2015573 {ECO:0000313|EMBL:OYU67594.1, ECO:0000313|Proteomes:UP000215757};
RN   [1] {ECO:0000313|EMBL:OYU67594.1, ECO:0000313|Proteomes:UP000215757}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCCC1 {ECO:0000313|EMBL:OYU67594.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L.,
RA   Hubert P., Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M.,
RA   Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom
RT   Asterionella formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:OYU67594.1}.
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DR   EMBL; NKJF01000005; OYU67594.1; -; Genomic_DNA.
DR   Proteomes; UP000215757; Unassembled WGS sequence.
DR   GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
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; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Complete proteome {ECO:0000313|Proteomes:UP000215757};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215757};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN        3     78       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      125    165       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   421 AA;  46888 MW;  93152A4158C07732 CRC64;
     MAKVEILMPS MGESIFECTV LKWLVNEGDH VEIDDMILEV ATDKIDTEIG SSHNGYITKF
     LVNDGDVALI GRPICEIETE SDAVVSKPTE KAPAIIEDEY VEQIEKAFEE VITSPSLVAS
     TNTKFYSPLV LNIAKKENIS QAELDNIKGT GFEKRVTKDD ILNFLNSKKQ PKTFVSEAPV
     ISRTGEDQIV EMDRMRKMIS QRMLESKAIS PHVTSFMETD MTSVVNWRLR IKDSFIKEFK
     ENLTFTPILI EAVVNAIKKY PGINIQVSGE NIIYKKDINI GMAVALPNGN LIVPVIHQAD
     KYSLSQLAVK VNDLAKRARN NQLKPEELSG GTYTITNIGT FGNLSGTPII MQPQVAIMAF
     GVIRKLPSVI ETSEGDLIGI RQKMVISHSF DHRVVDGSLG GLFLKEVSDF FENFDTKRVL
     N
//
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