ID A0A0H4VKL7_9BACT Unreviewed; 451 AA.
AC A0A0H4VKL7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=TH63_13075 {ECO:0000313|EMBL:AKQ46345.1};
OS Rufibacter radiotolerans.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Rufibacter.
OX NCBI_TaxID=1379910 {ECO:0000313|EMBL:AKQ46345.1, ECO:0000313|Proteomes:UP000036458};
RN [1] {ECO:0000313|EMBL:AKQ46345.1, ECO:0000313|Proteomes:UP000036458}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DG31D {ECO:0000313|EMBL:AKQ46345.1,
RC ECO:0000313|Proteomes:UP000036458};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Rufibacter sp./DG31D/ whole genome sequencing.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; CP010777; AKQ46345.1; -; Genomic_DNA.
DR RefSeq; WP_048921328.1; NZ_CP010777.1.
DR AlphaFoldDB; A0A0H4VKL7; -.
DR STRING; 1379910.TH63_13075; -.
DR KEGG; ruf:TH63_13075; -.
DR PATRIC; fig|1379910.4.peg.2839; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000036458; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR CDD; cd06849; lipoyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
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; 1.
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; 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 Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Reference proteome {ECO:0000313|Proteomes:UP000036458};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 3..78
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 130..170
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 81..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 180..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 48265 MW; 82518FF8E7F700CF CRC64;
MALVEMVMPK MGESIMEGTV LKWLKQVGDT IEQDESVLEV ATDKVDTEVP AIQAGILKEI
LVQEGQVVAV GAPIAIISTG GEDQPSAAPA AEQAAPAAQP TTQPAAHPAE APQATAQTSQ
RLEQPASGRF YSPLVMNIAR EEGITMQELE FVPGTGNEGR VTKKDILEYV VNRQSGAAPA
AAQPAAAQPQ APASQAAPQQ AAPAPSVPAP AQSYSGDAEI IEMDRMRKMI AQRMVDSKRI
SPHVTSFVEA DVTNIVNWRN KNKDAYKKRE GENLTFTPIF IEAIVKAIKD FPMINVSVDG
DRIIKKRNIN IGVAVALPSG NLIVPVIHNA DQMNLNGISK KLNDLANRAR INKLTAADLA
DPTYTVSNVG SFGNVMGTPI IMQPQVAIMA VGAIKKKPAV IETPEGDLIG IRQFMFLSHS
YDHRVVDGSL GGNFVRRVAD YLEGFDPNTA I
//
