ID A0A1T3DJF0_9FLAO Unreviewed; 528 AA.
AC A0A1T3DJF0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=BBD32_16540 {ECO:0000313|EMBL:AQX02950.1};
OS Elizabethkingia anophelis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Elizabethkingia.
OX NCBI_TaxID=1117645 {ECO:0000313|EMBL:AQX02950.1, ECO:0000313|Proteomes:UP000190848};
RN [1] {ECO:0000313|EMBL:AQX02950.1, ECO:0000313|Proteomes:UP000190848}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F3201 {ECO:0000313|EMBL:AQX02950.1,
RC ECO:0000313|Proteomes:UP000190848};
RA Nicholson A.C.;
RT "Revisiting the taxonomy of the Elizabethkingia Genus using Whole-Genome
RT Sequencing, Optical Mapping, and MALDI-TOF, along with proposal of three
RT novel Elizabethkingia species: Elizabethkingia bruuniana sp. nov.,
RT Elizabethkingia ursingii sp. nov., and Elizabethkingia occulta sp. nov.";
RL Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] = CoA
CC + N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein];
CC Xref=Rhea:RHEA:17017, Rhea:RHEA-COMP:10475, Rhea:RHEA-COMP:10478,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83111; EC=2.3.1.12;
CC Evidence={ECO:0000256|ARBA:ARBA00043782};
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; CP016374; AQX02950.1; -; Genomic_DNA.
DR RefSeq; WP_009084561.1; NZ_RSAY01000001.1.
DR GeneID; 56683086; -.
DR KEGG; een:BBD30_16850; -.
DR Proteomes; UP000190848; Chromosome.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
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; IPR045257; E2/Pdx1.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1.
DR PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE 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 Pyruvate {ECO:0000313|EMBL:AQX02950.1};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT REGION 94..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 528 AA; 55428 MW; 260E93BAFFB89540 CRC64;
MAEVITMPRL SDTMTEGKVS KWHKNVGDTV KEGDLLAEIE TDKAVQDFES EINGTLLYQG
VAEGGQAPVD TVLCIIGKEG EDISALIGGA PAKEEAPAQP VAEPAATEST ASAEVPAGVE
IITMPRLSDT MTEGKVAKWH KNVGDAVKEG DILAEIETDK AVQDFESEFN GTLLYQGVAE
SGAALVDTVL AIIGPAGTDV SGLTSGKPAA KSDAAPAASE KPVATQPKEE VVATSSTGDR
VAISPLARKI ASDKGIDIST VKGSGDGGRI VKKDIENYQP SAQAATSTAT VAPAKAVVNF
VAGEDTETPN SQVRNVIAKR LSESKFTAPH YYLMVEINMD KAIAARKEIN SLPDTKVSFN
DMIIKATAIA LRKHPQVNSS WAGDKIIHRG NINIGVAVAI PDGLVVPVLK NTDHMSYSEI
SASVKDMAAR AKNKGLKANE MEGSTFSISN LGMFGIETFT SIINQPNAAI LSVGAIIEKP
VVKDGQIVVG NTMKLSLACD HRVVDGATGA QFLQTLRTYL ENPLSLLV
//
