ID C6KUA0_9BACT Unreviewed; 549 AA.
AC C6KUA0;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 22-FEB-2023, entry version 47.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:BAH89548.1};
RN [1] {ECO:0000313|EMBL:BAH89548.1}
RP NUCLEOTIDE SEQUENCE.
RA Suenaga H., Ohnuki T., Miyazaki K.;
RT "Functional screening of a metagenomic library for genes involved in
RT microbial degradation of aromatic compounds.";
RL Environ. Microbiol. 9:2289-2297(2007).
RN [2] {ECO:0000313|EMBL:BAH89548.1}
RP NUCLEOTIDE SEQUENCE.
RA Suenaga H., Koyama Y., Miyakoshi M., Miyazaki R., Yano H., Sota M.,
RA Ohtsubo Y., Tsuda M., Miyazaki K.;
RT "Novel organization of aromatic degradation pathway genes in a microbial
RT community as revealed by metagenomic analysis.";
RL ISME J. 0:0-0(2009).
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938,
CC ECO:0000256|RuleBase:RU003423};
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU003423}.
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DR EMBL; AB266119; BAH89548.1; -; Genomic_DNA.
DR AlphaFoldDB; C6KUA0; -.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 2.
DR Gene3D; 2.40.50.100; -; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 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 PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF5; LIPOAMIDE ACYLTRANSFERASE COMPONENT OF BRANCHED-CHAIN ALPHA-KETO ACID DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS00189; LIPOYL; 2.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:BAH89548.1}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 125..200
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 262..299
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 233..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 549 AA; 57164 MW; 1480F90FD3D45EFE CRC64;
MNILAVKLPD VGEGVTAAEL VEWHVKVGDM VREDDTLAAV MTDKATVEIP SLYSGTVTWI
GGEVGDTLAV GSDLVRIETD AEAPVEAARA DEPAPVAVPE TVTPATKDAP VAATEKPVAP
AGKVIVAVKL PDVGEGVTEA ELAEWNVAIG DIVQEDDVIA AVMTDKATVE IPSLYSGKVV
GLGGSVGEVL AVGSDLVLIE TEAGAGSSGN APSPVSASAQ AAKAEVAKPA VQVQAAEAKP
SPARATATPA TGAPRAEGQP PLASPSVRAR AREAGLDLRQ IAGSGPAGRI THADIDAVFD
MSRRSPGQAA PAGRIARTGT EEIKVIGMRR KIAERMALAN ARIPHITVVE EVDVTALEEL
REKLNAGRGD KPKLTVLPFV TATLAKAMLD HPEMNAHYLD DDGIILRHAA VNAGIATMTD
AGLVVPVLRN AEALNLFETA AEIARLSEAA RTGKAKRDEL TGSTFTITSL GPLGALATTP
IINHPEVAIL GINKMAIRPM WDGTQFVPRK MMNISASFDH RVIDGWDAAV FVQRIKSLLE
TPALIFMES
//