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Database: UniProt
Entry: A0A1G6P5I4_9BURK
LinkDB: A0A1G6P5I4_9BURK
Original site: A0A1G6P5I4_9BURK 
ID   A0A1G6P5I4_9BURK        Unreviewed;       375 AA.
AC   A0A1G6P5I4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   16-JAN-2019, entry version 6.
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=SAMN05216345_103541 {ECO:0000313|EMBL:SDC74697.1};
OS   Cupriavidus sp. YR651.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1855315 {ECO:0000313|EMBL:SDC74697.1, ECO:0000313|Proteomes:UP000198719};
RN   [1] {ECO:0000313|EMBL:SDC74697.1, ECO:0000313|Proteomes:UP000198719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR651 {ECO:0000313|EMBL:SDC74697.1,
RC   ECO:0000313|Proteomes:UP000198719};
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; FMYZ01000003; SDC74697.1; -; Genomic_DNA.
DR   Proteomes; UP000198719; 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:UP000198719};
KW   Lipoyl {ECO:0000256|RuleBase:RU003423, ECO:0000256|SAAS:SAAS00065550};
KW   Pyruvate {ECO:0000313|EMBL:SDC74697.1};
KW   Transferase {ECO:0000256|RuleBase:RU003423,
KW   ECO:0000313|EMBL:SDC74697.1}.
FT   DOMAIN        1     76       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      115    152       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
SQ   SEQUENCE   375 AA;  38882 MW;  9CF54AB798F14871 CRC64;
     MRIFKLPDLG EGLQEAEIVT WHVKAGDTVA ADQPLLSVET AKAIVEIPSP FGGQVAKLFA
     QPGDIVHLGA PLVGFEGAGS TSDDAGTVVG AVKVGTQVVA EAAAPVGPGG AHGIKATPAV
     RALARKLSVD LAMVTPSGTD GLITATDVQR VATTLAEIGP AEVVRGVRRA MAQNMARAQS
     EVAAATVMDD ADLHAWQSTG ESGIATDITI RLVRALVAGV HAEPGLNAWY EGQTGRRHVL
     ERIDVGIAAD LPEGLFVPVL RNVGKRVAAD LRAGLDRMRA DIIARTIAPE EMRGNTITLS
     NFGMIAGRYA APIVVPPTVA ILGAGRIRDE VVAAGGVPAV HRVMPLSLTF DHRVVTGGEA
     ARFLRAVIAD LERPA
//
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