ID A0A1E5T952_9FLAO Unreviewed; 533 AA.
AC A0A1E5T952;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=A8C32_15615 {ECO:0000313|EMBL:OEK07903.1};
OS Flavivirga aquatica.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavivirga.
OX NCBI_TaxID=1849968 {ECO:0000313|EMBL:OEK07903.1, ECO:0000313|Proteomes:UP000095713};
RN [1] {ECO:0000313|EMBL:OEK07903.1, ECO:0000313|Proteomes:UP000095713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-16 {ECO:0000313|EMBL:OEK07903.1,
RC ECO:0000313|Proteomes:UP000095713};
RA Wong S.-K., Yoshizawa S., Nakajima Y., Ogura Y., Tetsuya H., Hamasaki K.;
RT "Draft Genome Sequence of Algibacter sp. Strain SK-16 Isolated from the
RT Surface Water of Aburatsubo Inlet.";
RL Submitted (MAY-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}.
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:OEK07903.1}.
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DR EMBL; MDJD01000043; OEK07903.1; -; Genomic_DNA.
DR RefSeq; WP_069830361.1; NZ_MDJD01000043.1.
DR AlphaFoldDB; A0A1E5T952; -.
DR STRING; 1849968.A8C32_15615; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000095713; 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:OEK07903.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095713};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 120..195
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 254..291
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 533 AA; 57023 MW; A961E2EAB6F4F327 CRC64;
MAIVVNMPRL SDTMEEGTVA AWLKKVGDKI EEGDILAEIE TDKATMEFES FNEGTLLHIG
VQEGETTKVD ELLAIIGDAG EDISGLLNGG SASVEVKEEP KKDEVVEEAT ASSVELPEGV
IVVTMPRLSD TMEEGTVATW LKKVGDVVEE GDILAEIETD KATMEFESFQ SGTLLEIGLQ
EGESAKVDAL LAIIGPAGTD ISGVAANFSV VVSSDKKEAP KVEAKKEVVK LEPVAASSKK
APIPTPVTEN GRIYVSPLAK KLAEEKGINL TKVQGTGENG RVVKRDIENY EPAAGAAAVG
KFVPAGQEDF EEVPNSQMRK AIAKALTNSK FSAPHYYLNV EFDMENAIAF RKQFNSIPDT
KISYNDMVVK ACALALKQHP QVNSQWFADK MRLNNHVHVG VAVAVPDGLV VPVVKFANEQ
TLPQIGAAVK DLAGKARNKK LTPAEMDGST FTVSNLGMFG IDTFTSIINQ PNSAILSVGN
IVEKPVVKDG QIVVGNTMKL SLACDHRTID GATGAQFLQT LKGYIENPVT MLV
//
