ID D6CVH6_THIA3 Unreviewed; 461 AA.
AC D6CVH6;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137};
DE EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137};
GN Name=aceF {ECO:0000313|EMBL:CAZ89295.1};
GN OrderedLocusNames=THI_2679 {ECO:0000313|EMBL:CAZ89295.1};
OS Thiomonas arsenitoxydans (strain DSM 22701 / CIP 110005 / 3As).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Thiomonas.
OX NCBI_TaxID=426114 {ECO:0000313|EMBL:CAZ89295.1, ECO:0000313|Proteomes:UP000002372};
RN [1] {ECO:0000313|Proteomes:UP000002372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22701 / CIP 110005 / 3As
RC {ECO:0000313|Proteomes:UP000002372};
RX PubMed=20195515; DOI=10.1371/journal.pgen.1000859;
RA Arsene-Ploetze F., Koechler S., Marchal M., Coppee J.Y., Chandler M.,
RA Bonnefoy V., Brochier-Armanet C., Barakat M., Barbe V.,
RA Battaglia-Brunet F., Bruneel O., Bryan C.G., Cleiss-Arnold J.,
RA Cruveiller S., Erhardt M., Heinrich-Salmeron A., Hommais F., Joulian C.,
RA Krin E., Lieutaud A., Lievremont D., Michel C., Muller D., Ortet P.,
RA Proux C., Siguier P., Roche D., Rouy Z., Salvignol G., Slyemi D., Talla E.,
RA Weiss S., Weissenbach J., Medigue C., Bertin P.N.;
RT "Structure, function, and evolution of the Thiomonas spp. genome.";
RL PLoS Genet. 6:E1000859-E1000859(2010).
CC -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC (E3). {ECO:0000256|ARBA:ARBA00025211}.
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 ECO:0000256|RuleBase:RU361137};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|RuleBase:RU361137};
CC Note=Binds 1 lipoyl cofactor covalently.
CC {ECO:0000256|RuleBase:RU361137};
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. {ECO:0000256|ARBA:ARBA00011484,
CC ECO:0000256|RuleBase:RU361137}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361137}.
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DR EMBL; FP475956; CAZ89295.1; -; Genomic_DNA.
DR AlphaFoldDB; D6CVH6; -.
DR KEGG; thi:THI_2679; -.
DR eggNOG; COG0508; Bacteria.
DR HOGENOM; CLU_016733_10_0_4; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000002372; Chromosome.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:UniProtKB-UniRule.
DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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; IPR006256; AcTrfase_Pyrv_DH_cplx.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR01348; PDHac_trf_long; 1.
DR PANTHER; PTHR43178; DIHYDROLIPOAMIDE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 1.
DR PANTHER; PTHR43178:SF2; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX; 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:RU361137,
KW ECO:0000313|EMBL:CAZ89295.1};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU361137};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Pyruvate {ECO:0000313|EMBL:CAZ89295.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002372};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:CAZ89295.1}.
FT DOMAIN 3..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 150..187
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 461 AA; 47901 MW; EAFCD09B78F5BBB0 CRC64;
MAVVEVKVPD IGDFKDVEVI EVLVKAGDQI AVDQSLVTVE SDKASMEIPS SAAGVVKALR
VKLGDKVSEG SVLLELDAAG AADALPAAEA PSAPVVPAAA EPAQPEASPP VALPPAAVGV
GFASEPRQHT PPTAALPVHE PAATTALLPH ASPSVRKLAR ELGVPLAEVK GSGSKGRITA
EDVQAFVKAV MSGQTVTQAA VVAGVGAGKG AASLGGLTLL PWPKVDFAKF GPVSSQPLSR
IKKLSGPNLA RNWAMIPHVT QFDEADITEL EDFRKSSNER MAKQGVKLTM LAFVMKACVT
VLKQMPAFNS SLDESGENLI LKDYIHLGFA ADTPQGLVVP VLKDVDKKGL AQIAKEMGEL
AATAREGKLK PSDMQGATFT ISSLGGVGGT AFTPIINAPE VAILGLSKSQ IKPVWDGAAF
QPRLMLPLSL SYDHRVIDGA MAARFTTVLG ELLADLRRVL I
//
