ID A0A1N7LH65_9FLAO Unreviewed; 533 AA.
AC A0A1N7LH65;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=B0A70_02890 {ECO:0000313|EMBL:PQA97624.1},
GN SAMN05421796_102316 {ECO:0000313|EMBL:SIS73133.1};
OS Chryseobacterium piscicola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=551459 {ECO:0000313|EMBL:SIS73133.1, ECO:0000313|Proteomes:UP000186246};
RN [1] {ECO:0000313|EMBL:PQA97624.1, ECO:0000313|Proteomes:UP000238314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21068 {ECO:0000313|EMBL:PQA97624.1,
RC ECO:0000313|Proteomes:UP000238314};
RA Stine C., Li C., Tadesse D.;
RT "Whole genomes of Flavobacteriaceae.";
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SIS73133.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21068 {ECO:0000313|EMBL:SIS73133.1};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000186246}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21068 {ECO:0000313|Proteomes:UP000186246};
RA Varghese N., Submissions S.;
RL Submitted (JAN-2017) 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; MUGO01000002; PQA97624.1; -; Genomic_DNA.
DR EMBL; FTOJ01000002; SIS73133.1; -; Genomic_DNA.
DR RefSeq; WP_076450671.1; NZ_MUGO01000002.1.
DR AlphaFoldDB; A0A1N7LH65; -.
DR STRING; 551459.SAMN05421796_102316; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000186246; Unassembled WGS sequence.
DR Proteomes; UP000238314; Unassembled WGS sequence.
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:SIS73133.1};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:SIS73133.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 124..199
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 246..283
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 84..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 533 AA; 56621 MW; 7F3BB1DCA7D1CBAC CRC64;
MAEVITMPRL SDTMTEGKVA KWHKKVGDKV KEGDILAEIE TDKAVQDFES EIEGTLLYVG
VEEGSAAAVD LVLAIIGNEG EDISGLTGGA SAPAANATED KKEEAQPEAK NETQAAIAEV
PKGVEVITMP RLSDTMTEGK VAKWHKNVGD TVKEGDLLAE IETDKAVQDF ESEFNGILLK
QGVEEGGAAP VDTVLAIIGP EGTDVSGVNS PKSTQHSSAQ PEEQKNESKV EEKSVAQVTV
SSDRVAISPL AKKMAQDKGV DISGVQGSGE NGRIVKKDIE NYQPSAKPAT ENAAPVAAAQ
VAVNFVQGED SETPNSQVRN IIAKRLAESK FSAPHYYLMV EINMDKAIAA RKEINALPDT
KISFNDMIIK ATAIALRKHP QVNSSWAGDK IIHRGNINIG VAVAIPDGLV VPVLKNTDQM
SYTQISAGVK DMAGRAKSKG LKANEMEGST FSISNLGMFG IETFTSIINQ PNSAILSVGA
IIEKPIVKDG QIVVGNTMKL SLACDHRVVD GATGAQFLQT LRTYLENPLS LLV
//
