ID A0A2H5F5U0_9RHOB Unreviewed; 426 AA.
AC A0A2H5F5U0;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:AUH66909.1};
GN ORFNames=CX676_21620 {ECO:0000313|EMBL:AUH66909.1};
OS Paracoccus zhejiangensis.
OG Plasmid ppz03 {ECO:0000313|Proteomes:UP000234530}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1077935 {ECO:0000313|EMBL:AUH66909.1, ECO:0000313|Proteomes:UP000234530};
RN [1] {ECO:0000313|EMBL:AUH66909.1, ECO:0000313|Proteomes:UP000234530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J6 {ECO:0000313|EMBL:AUH66909.1,
RC ECO:0000313|Proteomes:UP000234530};
RC PLASMID=Plasmid ppz03 {ECO:0000313|Proteomes:UP000234530};
RX PubMed=23653121; DOI=10.1007/s10482-013-9932-2;
RA Wu Z.G., Zhang D.F., Liu Y.L., Wang F., Jiang X., Li C., Li S.P., Hong Q.,
RA Li W.J.;
RT "Paracoccus zhejiangensis sp. nov., isolated from activated sludge in
RT wastewater-treatment system.";
RL Antonie Van Leeuwenhoek 104:123-128(2013).
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; CP025433; AUH66909.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5F5U0; -.
DR KEGG; pzh:CX676_21620; -.
DR OrthoDB; 9805770at2; -.
DR Proteomes; UP000234530; Plasmid ppz03.
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 Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU361137};
KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137};
KW Plasmid {ECO:0000313|EMBL:AUH66909.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000234530};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU361137, ECO:0000313|EMBL:AUH66909.1}.
FT DOMAIN 2..76
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 125..162
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
SQ SEQUENCE 426 AA; 44422 MW; 0103A93054AFD6DB CRC64;
MPVEVNVPDI GDFKDVPVIT VLVKVGDTVA AEDPLIELES DKATMEVPSP VAGRIASIVV
KEGDRVSEGS VILTVEAEGS DAAAAASAPA SAPAAAPVAA PAASAPVAAA PAAAAVTDSG
FNKAHASPSI RAFARQLGID LAKINGSGRK GRILRDDVTA ALKASAVPAA AASGGAAQGG
GMGIPPIPVV DFSKFGPVEN VEMPRIKKLS GPALHRSWLN VPHVTHQEEA DITEIDQFRK
ELDDEAKKDG YRVTLLALVI KASVSALRKH WEFNSSIHPD GDKLIRKSYY NIGFAADTPN
GLVVPVIKDA DRKGIVDISK ELGDLSAKAR AGELKSQDMQ GATFTISSLG GIGGTAFTPI
VNAPEVAILG LTRSRMAPVW DGQQFVPRNM LPMSLSYDHR AIDGALAARF AATLKHLLGD
VRRIML
//
