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Database: UniProt
Entry: A0A1H3KYW2_9BACI
LinkDB: A0A1H3KYW2_9BACI
Original site: A0A1H3KYW2_9BACI 
ID   A0A1H3KYW2_9BACI        Unreviewed;       425 AA.
AC   A0A1H3KYW2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   31-JUL-2019, entry version 8.
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=SAMN05421736_102308 {ECO:0000313|EMBL:SDY57427.1};
OS   Bacillus caseinilyticus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1503961 {ECO:0000313|EMBL:SDY57427.1, ECO:0000313|Proteomes:UP000198935};
RN   [1] {ECO:0000313|EMBL:SDY57427.1, ECO:0000313|Proteomes:UP000198935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SP {ECO:0000313|EMBL:SDY57427.1,
RC   ECO:0000313|Proteomes:UP000198935};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FNPI01000002; SDY57427.1; -; Genomic_DNA.
DR   BioCyc; GCF_900107275:BLU90_RS06675-MONOMER; -.
DR   Proteomes; UP000198935; 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; IPR003016; 2-oxoA_DH_lipoyl-BS.
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; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW   Complete proteome {ECO:0000313|Proteomes:UP000198935};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198935};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN        2     77       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      118    155       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       82    118       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
SQ   SEQUENCE   425 AA;  46565 MW;  069E33662454DAF1 CRC64;
     MATEITMPQL GESVTEGTIT KWLVKPGDKV NKYDPLAEVM TDKVNAEIPS SFSGTIKELI
     AQEDQTLGVG EVICTLVTEA EGQAAPTAGT TEPEKAEPAA EAPLHASTSQ DESENKRRYS
     PAVMRLAQEN NIDLEQVQGS GRGGRITRKD LLAVIASGHL LEQKEATSTL APAAAEVQRQ
     TAAVKTVSVP SGKVEEIPVS GVRRAIANNM VKSKQEAPHA WMMIEVDVTE LVRYRNKIKE
     QFSKKEGIKL TFLPFFVKAV VDALKEYPEI NSMWAGEKII RHRDIHISLA VATETELYVP
     VIKHADEKSI KGLAKEMDSL VQKVRTKSLK QEDMTGGTFT VNNTGSFGSI QSQPIINQPQ
     AAILSVEAIV KRPVVLENDA IAVRHMVNLC MSLDHRVLDG LICGKFLGHI KNTLENIREE
     NTPIY
//
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