ID A0A0M8JPQ0_9CHLR Unreviewed; 418 AA.
AC A0A0M8JPQ0;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=ADN01_16905 {ECO:0000313|EMBL:KPL76228.1}, LSAC_02900
GN {ECO:0000313|EMBL:GAP19002.1};
OS Levilinea saccharolytica.
OC Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC Levilinea.
OX NCBI_TaxID=229921 {ECO:0000313|EMBL:GAP19002.1};
RN [1] {ECO:0000313|EMBL:GAP19002.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=KIBI-1 {ECO:0000313|EMBL:GAP19002.1};
RA Matsuura N., Tourlousse M.D., Ohashi A., Hugenholtz P., Sekiguchi Y.;
RT "Draft Genome Sequences of Anaerolinea thermolimosa IMO-1, Bellilinea
RT caldifistulae GOMI-1, Leptolinea tardivitalis YMTK-2, Levilinea
RT saccharolytica KIBI-1, Longilinea arvoryzae KOME-1, Previously Described as
RT Members of the Class Anaerolineae (Chloroflexi).";
RL Genome Announc. 3:e00975-15(2015).
RN [2] {ECO:0000313|EMBL:KPL76228.1, ECO:0000313|Proteomes:UP000050501}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIBI-1 {ECO:0000313|EMBL:KPL76228.1,
RC ECO:0000313|Proteomes:UP000050501};
RA Hemp J., Ward L.M., Pace L.A., Fischer W.W.;
RT "Genome sequence of Levilinea saccharolytica DSM 16555.";
RL Submitted (JUL-2015) 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; DF967975; GAP19002.1; -; Genomic_DNA.
DR EMBL; LGCM01000064; KPL76228.1; -; Genomic_DNA.
DR RefSeq; WP_062419313.1; NZ_LGCM01000064.1.
DR AlphaFoldDB; A0A0M8JPQ0; -.
DR STRING; 229921.ADN01_16905; -.
DR PATRIC; fig|229921.5.peg.1782; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000050501; 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; 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; 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; 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 ECO:0000313|EMBL:GAP19002.1};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU003423};
KW Pyruvate {ECO:0000313|EMBL:GAP19002.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050501};
KW Transferase {ECO:0000256|RuleBase:RU003423, ECO:0000313|EMBL:GAP19002.1}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 126..163
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 418 AA; 43328 MW; B5E34226ACC08A82 CRC64;
MAEIVSMPKL GFDMAEGTLV RWVKNEGDTI AKGDVLAEIE TDKATVEVES SFSGVVARHL
VEAGAIVPVG TPIAVIGAEG EEVKDVPGLS GTPEKAVAPA AAAPAPAAPA ASQPAAAAPV
SSGPVVASPL ARRIAADNGL DLAAVRGTGP GGRIVKRDVE AALKAGPAAV SALAAPAATI
PAAVPAAAAR ADEVVGLDRL RVAIGRRMTE SKQQLPHFYV THEYDMEALL GLRKQVNALL
PEEDKLSVND FIVKAVGLCL RRFPNLNASL KEGQLVRHGA VNVGVAVAVE GGLLTIVTRA
TDAKPLRTLS GEIRDLVSRA RSGKVRPDDI EGSTFSISNL GMYDVEHFIA IINPPEAAIL
AVGSAREVPV VKDGQVTVGL RMKATLSADH RVTDGAEAAQ FMQALADYLE QPLRLLVE
//
