ID A0A2R7KBU1_9SPHI Unreviewed; 551 AA.
AC A0A2R7KBU1;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=DBR11_22190 {ECO:0000313|EMBL:PTS94978.1};
OS Pedobacter sp. HMWF019.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=2056856 {ECO:0000313|EMBL:PTS94978.1, ECO:0000313|Proteomes:UP000244301};
RN [1] {ECO:0000313|EMBL:PTS94978.1, ECO:0000313|Proteomes:UP000244301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMWF019 {ECO:0000313|EMBL:PTS94978.1,
RC ECO:0000313|Proteomes:UP000244301};
RA Go L.Y., Mitchell J.A.;
RL Submitted (APR-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PTS94978.1}.
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DR EMBL; QAIL01000412; PTS94978.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R7KBU1; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000244301; Unassembled WGS sequence.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:RHEA.
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:PTS94978.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244301};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 131..206
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 259..296
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 89..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 57604 MW; DF1909CA89803814 CRC64;
MAEVVRMPKM SDTMTEGVMA KWHKKVGDKV KSGDVMAEVE TDKATMDLES YWDGTILYIG
VEEGKAVPVD AVIAVVGKEG EDYKAALEAE GAGSPAAAPA AEAKTEETPA APAENKASSG
LSEAELTKQG VTVVRMPLLS DTMTEGVIAE WHKKVGDKVK EDDILADVET DKATMEVMGY
AEGTLLHIGV EKGQAAKVNG IIAIVGPEGT DISGILSQGT APAVAADKKS DAPVAEKANT
ADVPAAAHEA VTADGGRVKA SPLAKRIAKE KGIDLSQVAG SADGGRIIKK DIENFKPAAA
TASTASSSAP AAEKTAPVIP AYVGEVKFTE KPVSQMRKVI AKRLAESLFT APHFYLNISI
DMDNAIAART AINTVAPVKV SFNDIIIKAV AVALKQHPAV NSSWLGDKIR FNEHTNIGVA
MAVEDGLLVP VVRFADGKSL SHISAEVKEY GQKAKAKKLQ PADWEGSTFT VSNLGMFGID
EFTSIINSPD GAILSVGAIQ QIPVVKNGAV VPGNVMKLSL GCDHRVVDGA TGAAFLQTLK
GLLEEPIRLL V
//
