ID Q2GIM3_ANAPZ Unreviewed; 420 AA. AC Q2GIM3; DT 21-MAR-2006, integrated into UniProtKB/TrEMBL. DT 21-MAR-2006, sequence version 1. DT 04-NOV-2026, entry version 118. DE RecName: Full=Acetyltransferase component of pyruvate dehydrogenase complex {ECO:0000256|RuleBase:RU361137}; DE EC=2.3.1.12 {ECO:0000256|RuleBase:RU361137}; GN OrderedLocusNames=APH_1257 {ECO:0000313|EMBL:ABD43974.1}; OS Anaplasma phagocytophilum (strain HZ). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rickettsiales; Anaplasmataceae; Anaplasma; phagocytophilum group. OX NCBI_TaxID=212042 {ECO:0000313|EMBL:ABD43974.1, ECO:0000313|Proteomes:UP000001943}; RN [1] {ECO:0000313|EMBL:ABD43974.1, ECO:0000313|Proteomes:UP000001943} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HZ {ECO:0000313|EMBL:ABD43974.1, RC ECO:0000313|Proteomes:UP000001943}; RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021; RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W., RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J., Daugherty S.C., RA Davidsen T., Durkin A.S., Gwinn M., Haft D.H., Selengut J.D., RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.; RT "Comparative genomics of emerging human ehrlichiosis agents."; RL PLoS Genet. 2:208-222(2006). 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=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + acetyl-CoA = CC N(6)-[(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein] + CoA; 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:ARBA00048370, 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 -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361137}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000235; ABD43974.1; -; Genomic_DNA. DR RefSeq; WP_011451285.1; NC_007797.1. DR AlphaFoldDB; Q2GIM3; -. DR STRING; 212042.APH_1257; -. DR PaxDb; 212042-APH_1257; -. DR EnsemblBacteria; ABD43974; ABD43974; APH_1257. DR GeneID; 92747862; -. DR KEGG; aph:APH_1257; -. DR PATRIC; fig|212042.8.peg.1349; -. DR eggNOG; COG0508; Bacteria. DR HOGENOM; CLU_016733_10_2_5; -. DR OMA; AAKFLNC; -. DR Proteomes; UP000001943; 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:0006086; P:pyruvate decarboxylation to acetyl-CoA; IEA:InterPro. DR CDD; cd06849; lipoyl_domain; 1. DR FunFam; 2.40.50.100:FF:000010; Acetyltransferase component of pyruvate dehydrogenase complex; 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; IPR006257; LAT1. DR InterPro; IPR004167; PSBD. DR InterPro; IPR011053; Single_hybrid_motif. DR NCBIfam; TIGR01349; PDHac_trf_mito; 1. DR PANTHER; PTHR23151; DIHYDROLIPOAMIDE ACETYL/SUCCINYL-TRANSFERASE-RELATED; 1. DR PANTHER; PTHR23151:SF90; DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 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|ARBA:ARBA00023315, KW ECO:0000256|RuleBase:RU361137}; KW Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|RuleBase:RU361137}; KW Pyruvate {ECO:0000313|EMBL:ABD43974.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001943}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361137}. FT DOMAIN 2..79 FT /note="Lipoyl-binding" FT /evidence="ECO:0000259|PROSITE:PS50968" FT DOMAIN 145..182 FT /note="Peripheral subunit-binding (PSBD)" FT /evidence="ECO:0000259|PROSITE:PS51826" SQ SEQUENCE 420 AA; 44574 MW; 4761EFEDAD8EAB72 CRC64; MPVKVLMPAL SPTMKSGTIA KWHKNAGDAV KPGDIVADIE TDKAVIEFEY ADEPGVMYKI LKEEGSKNVA VNQSIAVIKV DGDEEAALLE MVHSAEGASG SVSNEAASAA LQATPAKVAG DMVAPSSANK ASETAHITSG SDRVKASPLA KKLAAQLSVD ISKITGSGPY GRVVKADVLG ASVPTSDTTI QEGSRVVEVS TMRKVISERL AESKRNIPHF YLAIDCMVGE LLEVRSRINS NAEALGTKIT VNDLVIKATA LAAREFPEVN ALWAGDKIVY HQNVDIAFAV ALDDGLLTPV IAGADKMTLS ELSKTAKSLV ARAKDRKLLP HEFQGGCLTI SNLGMFCIKE FYAIINPPQS CIMAVGQSEK RPVVVDNCVV AADVMSVTLS VDHRVIDGAL AAKFLNRFKF YIENPLAMLA //