ID D9TIY4_CALOO Unreviewed; 452 AA.
AC D9TIY4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU003423};
DE EC=2.3.1.- {ECO:0000256|RuleBase:RU003423};
GN OrderedLocusNames=COB47_0651 {ECO:0000313|EMBL:ADL41966.1};
OS Caldicellulosiruptor obsidiansis (strain ATCC BAA-2073 / strain OB47).
OC Bacteria; Bacillota; Clostridia; Caldicellulosiruptorales;
OC Caldicellulosiruptoraceae; Caldicellulosiruptor.
OX NCBI_TaxID=608506 {ECO:0000313|EMBL:ADL41966.1, ECO:0000313|Proteomes:UP000000347};
RN [1] {ECO:0000313|EMBL:ADL41966.1, ECO:0000313|Proteomes:UP000000347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2073 / strain OB47
RC {ECO:0000313|Proteomes:UP000000347};
RX PubMed=20851897; DOI=10.1128/JB.00950-10;
RA Elkins J.G., Lochner A., Hamilton-Brehm S.D., Davenport K.W., Podar M.,
RA Brown S.D., Land M.L., Hauser L.J., Klingeman D.M., Raman B., Goodwin L.A.,
RA Tapia R., Meincke L.J., Detter J.C., Bruce D.C., Han C.S., Palumbo A.V.,
RA Cottingham R.W., Keller M., Graham D.E.;
RT "Complete genome sequence of the cellulolytic thermophile
RT Caldicellulosiruptor obsidiansis OB47T.";
RL J. Bacteriol. 192:6099-6100(2010).
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; CP002164; ADL41966.1; -; Genomic_DNA.
DR RefSeq; WP_013289970.1; NC_014392.1.
DR AlphaFoldDB; D9TIY4; -.
DR STRING; 608506.COB47_0651; -.
DR KEGG; cob:COB47_0651; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_2_9; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000000347; 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; 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; 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; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU003423};
KW Lipoyl {ECO:0000256|RuleBase:RU003423};
KW Transferase {ECO:0000256|RuleBase:RU003423}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 128..165
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 452 AA; 50474 MW; E30409A94322A237 CRC64;
MATPVIMPKQ GQTVESCIIT KWYKKKGDKV EVGDLLFSYE TDKASFDEEA KVSGVLLDIF
FEEGEEVPVL TNVCVIGEPG EDVQHFNPKA SSEVQKVHIS HQTYEQDVPG ETQTKISKHY
SPIEGKIKIS PRAKNLAEKL NVDFRFAKPS GPDGRIIERD ILKLFESGPV FTSAATQEAK
EVEDVQILEP TGIGGRITTF DIERAKQESY VSKISESSGQ NVEYEDVPLS NIRKAIAKAM
YLSLTTTAQL TLHTSFDASK ILEFRKKVKE NREKLELEDI TINDIILFAV SRVLPKHKLL
NSHFLDDKMR YFKNVHLGFA VDTERGLMVP TIFNCNQKTL SQISKEAKEL IGLCRKGTIS
PDLLKGATFT ITNLGSFGIE SFTPVLNPPQ TGILGVNTIV QRSKEENGQI KFYPAMGLSL
TFDHRALDGA DAARFLKDLK ELLENFDLLL AL
//
