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Database: UniProt
Entry: I8AJT0_9BACI
LinkDB: I8AJT0_9BACI
Original site: I8AJT0_9BACI 
ID   I8AJT0_9BACI            Unreviewed;       410 AA.
AC   I8AJT0;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   10-APR-2019, entry version 32.
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=A374_08214 {ECO:0000313|EMBL:EIT85804.1};
OS   Fictibacillus macauensis ZFHKF-1.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX   NCBI_TaxID=1196324 {ECO:0000313|EMBL:EIT85804.1, ECO:0000313|Proteomes:UP000004080};
RN   [1] {ECO:0000313|EMBL:EIT85804.1, ECO:0000313|Proteomes:UP000004080}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZFHKF-1 {ECO:0000313|EMBL:EIT85804.1,
RC   ECO:0000313|Proteomes:UP000004080};
RX   PubMed=22887677; DOI=10.1128/JB.01049-12;
RA   Cai L., Zhang T.;
RT   "Genome of Bacillus macauensis ZFHKF-1, a Long-Chain-Forming
RT   Bacterium.";
RL   J. Bacteriol. 194:4780-4780(2012).
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:EIT85804.1}.
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DR   EMBL; AKKV01000024; EIT85804.1; -; Genomic_DNA.
DR   RefSeq; WP_007201736.1; NZ_AKKV01000024.1.
DR   STRING; 1196324.A374_08214; -.
DR   EnsemblBacteria; EIT85804; EIT85804; A374_08214.
DR   PATRIC; fig|1196324.3.peg.1686; -.
DR   OrthoDB; 1626282at2; -.
DR   Proteomes; UP000004080; 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:UP000004080};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004080};
KW   Transferase {ECO:0000256|RuleBase:RU003423}.
FT   DOMAIN        1     76       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      118    155       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   410 AA;  44899 MW;  BE5BA1DF7D58F638 CRC64;
     MVEVKLHDIG EGMHEGEILH FFVKPGDIVT IDQPLVEVQT DKVTAELPSP VAGKVSKLLV
     KEGETVTVGT VLLVLEGEGS SHAKKESQEP LGAAKQVTTV GNSPKDESAL ALLTKRILAA
     PYTRKLAREH QVDLELVTGT GPAGRITEED VMRFVAGDQK DNIVSAAALE EPQKDSSLST
     ATVSTIPFKG RRKQIAKKMT QSLFTIPHVT HFEEIDMTAL LEMKKQLKQN DTNVSVAAFF
     VKALQFALRD FPIFNSKLDE ANDVIQMHEQ INIGIATDAE DGLIVPVIHD IKALSIKEIN
     EDMKMKMEKA KNGTLSRQDM SNGTFTISNV GPLGSMGATP IINAPEVALM AFHKTKRVPV
     VMGEEIVIRS MMNVSMSFDH RVADGASAVM FTNRFKHFIE NPSFMLVEMV
//
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