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Database: UniProt
Entry: A0A1H7QEF8_9PSED
LinkDB: A0A1H7QEF8_9PSED
Original site: A0A1H7QEF8_9PSED 
ID   A0A1H7QEF8_9PSED        Unreviewed;       371 AA.
AC   A0A1H7QEF8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   13-FEB-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=SAMN05216214_112109 {ECO:0000313|EMBL:SEL45687.1};
OS   Pseudomonas hussainii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1429083 {ECO:0000313|EMBL:SEL45687.1, ECO:0000313|Proteomes:UP000185766};
RN   [1] {ECO:0000313|EMBL:SEL45687.1, ECO:0000313|Proteomes:UP000185766}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19513 {ECO:0000313|EMBL:SEL45687.1,
RC   ECO:0000313|Proteomes:UP000185766};
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; FOAS01000012; SEL45687.1; -; Genomic_DNA.
DR   RefSeq; WP_074869204.1; NZ_FOAS01000012.1.
DR   BioCyc; GCF_900109735:BMX80_RS12930-MONOMER; -.
DR   Proteomes; UP000185766; 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:UP000185766};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:SEL45687.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000185766};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:SEL45687.1}.
FT   DOMAIN        1     76       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      116    153       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   371 AA;  38952 MW;  BDD9F5B093389AE0 CRC64;
     MKTFKLPDLG EGLQEAEIVE WHVSAGETVK ADQLIVSVET AKAIVEIPSP CDGVIGKCHG
     GEGDILHVGE TLVTFEGGED DAGTVVGRLD AGGAAGSSDT FFVGAAPSSL EHQAPKASPA
     VRQLARRLDV DLAQLSGSGP EGLITRQDVE AAAEQSLAKF GGERLRGVRR TMAKNMARAH
     AEVVPVVIVE DADLHQWGEA RDPMIRLAQA IGVACQAEPL LNSWFDGKGP SLKEHAHVDL
     GIAVDTPDGL FVPVLRNITA RSGDELREGL GNLRAAVKAR SIPPHELLGA TITLSNFGTL
     FGRYANPVVV PPQVCIIGAG GIRQEPVAVN GKVEVHPILP LSLTFDHRAV TGGEAARFLK
     ALILALQAPE A
//
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