ID ODP2_AZOVI Reviewed; 638 AA. AC P10802; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 148. DE RecName: Full=Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex; DE EC=2.3.1.12; DE AltName: Full=Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex; DE AltName: Full=E2; OS Azotobacter vinelandii. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=354; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 478 / DSM 2289 / BCRC 14361 / JCM 21475 / KCTC 12137 / RC NBRC 102612 / NCIMB 12096 / NRRL B-14641 / VKM B-1617 / NRS 16; RX PubMed=3292237; DOI=10.1111/j.1432-1033.1988.tb14140.x; RA Hanemaaijer R., Janssen A., de Kok A., Veeger C.; RT "The dihydrolipoyltransacetylase component of the pyruvate dehydrogenase RT complex from Azotobacter vinelandii. Molecular cloning and sequence RT analysis."; RL Eur. J. Biochem. 174:593-599(1988). RN [2] RP PROTEIN SEQUENCE OF 2-16 AND 381-416. RX PubMed=3691494; DOI=10.1111/j.1432-1033.1987.tb13604.x; RA Hanemaaijer R., de Kok A., Jolles J., Veeger C.; RT "The domain structure of the dihydrolipoyl transacetylase component of the RT pyruvate dehydrogenase complex from Azotobacter vinelandii."; RL Eur. J. Biochem. 169:245-252(1987). RN [3] RP LIPOYL DOMAIN CONFORMATION. RX PubMed=3191993; DOI=10.1016/0014-5793(88)80369-7; RA Hanemaaijer R., Vervoort J., Westphal A.H., de Kok A., Veeger C.; RT "Mobile sequences in the pyruvate dehydrogenase complex, the E2 component, RT the catalytic domain and the 2-oxoglutarate dehydrogenase complex of RT Azotobacter vinelandii, as detected by 600 MHz 1H-NMR spectroscopy."; RL FEBS Lett. 240:205-210(1988). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 382-638. RX PubMed=1549782; DOI=10.1126/science.1549782; RA Mattevi A., Obmolova G., Schulze E., Kalk K.H., Westphal A.H., de Kok A., RA Hol W.G.J.; RT "Atomic structure of the cubic core of the pyruvate dehydrogenase RT multienzyme complex."; RL Science 255:1544-1550(1992). RN [5] RP STRUCTURE BY NMR OF 1-79. RX PubMed=8068086; DOI=10.1111/j.1432-1033.1994.tb18717.x; RA Berg A., de Kok A., Vervoort J.; RT "Sequential 1H and 15N nuclear magnetic resonance assignments and secondary RT structure of the N-terminal lipoyl domain of the dihydrolipoyl RT transacetylase component of the pyruvate dehydrogenase complex from RT Azotobacter vinelandii."; RL Eur. J. Biochem. 221:87-100(1994). RN [6] RP STRUCTURE BY NMR OF 1-79. RX PubMed=9119000; DOI=10.1111/j.1432-1033.1997.00352.x; RA Berg A., Vervoort J., de Kok A.; RT "Three-dimensional structure in solution of the N-terminal lipoyl domain of RT the pyruvate dehydrogenase complex from Azotobacter vinelandii."; RL Eur. J. Biochem. 244:352-360(1997). 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). 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 -!- COFACTOR: CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; Evidence={ECO:0000250}; CC Note=Binds 3 lipoyl cofactors covalently. {ECO:0000250}; CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral CC symmetry. CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=CAA30987.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; X12455; CAA30987.1; ALT_INIT; Genomic_DNA. DR PIR; S01017; XXAV. DR PDB; 1DPB; X-ray; 2.50 A; A=396-638. DR PDB; 1DPC; X-ray; 2.60 A; A=396-638. DR PDB; 1DPD; X-ray; 2.70 A; A=396-638. DR PDB; 1EAA; X-ray; 2.60 A; A=396-638. DR PDB; 1EAB; X-ray; 2.60 A; A=396-638. DR PDB; 1EAC; X-ray; 2.60 A; A=396-638. DR PDB; 1EAD; X-ray; 2.60 A; A=396-638. DR PDB; 1EAE; X-ray; 2.60 A; A=396-638. DR PDB; 1EAF; X-ray; 2.60 A; A=396-638. DR PDB; 1IYU; NMR; -; A=2-79. DR PDB; 1IYV; NMR; -; A=2-79. DR PDBsum; 1DPB; -. DR PDBsum; 1DPC; -. DR PDBsum; 1DPD; -. DR PDBsum; 1EAA; -. DR PDBsum; 1EAB; -. DR PDBsum; 1EAC; -. DR PDBsum; 1EAD; -. DR PDBsum; 1EAE; -. DR PDBsum; 1EAF; -. DR PDBsum; 1IYU; -. DR PDBsum; 1IYV; -. DR AlphaFoldDB; P10802; -. DR SMR; P10802; -. DR DrugBank; DB08120; 6,8-DIMERCAPTO-OCTANOIC ACID AMIDE. DR DrugBank; DB01992; Coenzyme A. DR DrugBank; DB01846; Oxidized coenzyme A. DR EvolutionaryTrace; P10802; -. DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IEA:InterPro. DR GO; GO:0004742; F:dihydrolipoyllysine-residue acetyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW. DR CDD; cd06849; lipoyl_domain; 3. DR Gene3D; 2.40.50.100; -; 3. 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; 3. 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; 3. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 3. DR PROSITE; PS00189; LIPOYL; 3. DR PROSITE; PS51826; PSBD; 1. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Direct protein sequencing; Lipoyl; Repeat; KW Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:3691494" FT CHAIN 2..638 FT /note="Dihydrolipoyllysine-residue acetyltransferase FT component of pyruvate dehydrogenase complex" FT /id="PRO_0000162272" FT DOMAIN 2..74 FT /note="Lipoyl-binding 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066" FT DOMAIN 117..191 FT /note="Lipoyl-binding 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066" FT DOMAIN 222..296 FT /note="Lipoyl-binding 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066" FT DOMAIN 338..375 FT /note="Peripheral subunit-binding (PSBD)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170" FT REGION 90..119 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 201..220 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 301..336 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 382..638 FT /note="Catalytic" FT ACT_SITE 611 FT /evidence="ECO:0000255" FT MOD_RES 40 FT /note="N6-lipoyllysine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066" FT MOD_RES 157 FT /note="N6-lipoyllysine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066" FT MOD_RES 262 FT /note="N6-lipoyllysine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066" FT STRAND 3..6 FT /evidence="ECO:0007829|PDB:1IYU" FT STRAND 11..19 FT /evidence="ECO:0007829|PDB:1IYU" FT STRAND 29..37 FT /evidence="ECO:0007829|PDB:1IYU" FT STRAND 42..46 FT /evidence="ECO:0007829|PDB:1IYU" FT STRAND 48..57 FT /evidence="ECO:0007829|PDB:1IYU" FT STRAND 63..65 FT /evidence="ECO:0007829|PDB:1IYU" FT STRAND 68..74 FT /evidence="ECO:0007829|PDB:1IYU" FT HELIX 404..406 FT /evidence="ECO:0007829|PDB:1DPB" FT HELIX 417..432 FT /evidence="ECO:0007829|PDB:1DPB" FT STRAND 435..443 FT /evidence="ECO:0007829|PDB:1DPB" FT HELIX 445..453 FT /evidence="ECO:0007829|PDB:1DPB" FT HELIX 455..460 FT /evidence="ECO:0007829|PDB:1DPB" FT HELIX 468..481 FT /evidence="ECO:0007829|PDB:1DPB" FT HELIX 483..486 FT /evidence="ECO:0007829|PDB:1DPB" FT STRAND 487..489 FT /evidence="ECO:0007829|PDB:1DPB" FT STRAND 496..498 FT /evidence="ECO:0007829|PDB:1DPB" FT STRAND 504..506 FT /evidence="ECO:0007829|PDB:1DPB" FT STRAND 508..510 FT /evidence="ECO:0007829|PDB:1DPB" FT STRAND 513..515 FT /evidence="ECO:0007829|PDB:1DPB" FT STRAND 518..520 FT /evidence="ECO:0007829|PDB:1EAA" FT HELIX 522..524 FT /evidence="ECO:0007829|PDB:1DPB" FT HELIX 527..542 FT /evidence="ECO:0007829|PDB:1DPB" FT HELIX 548..551 FT /evidence="ECO:0007829|PDB:1DPB" FT STRAND 555..560 FT /evidence="ECO:0007829|PDB:1DPB" FT TURN 562..564 FT /evidence="ECO:0007829|PDB:1DPB" FT STRAND 577..583 FT /evidence="ECO:0007829|PDB:1DPB" FT STRAND 587..592 FT /evidence="ECO:0007829|PDB:1DPB" FT STRAND 594..610 FT /evidence="ECO:0007829|PDB:1DPB" FT TURN 611..613 FT /evidence="ECO:0007829|PDB:1DPB" FT HELIX 616..631 FT /evidence="ECO:0007829|PDB:1DPB" FT HELIX 633..637 FT /evidence="ECO:0007829|PDB:1DPB" SQ SEQUENCE 638 AA; 65045 MW; 8B92CB5ADEA0BEA1 CRC64; MSEIIRVPDI GGDGEVIELL VKTGDLIEVE QGLVVLESAK ASMEVPSPKA GVVKSVSVKL GDKLKEGDAI IELEPAAGAA AAPAEAAAVP AAPTQAVDEA EAPSPGASAT PAPAAASQEV RVPDIGSAGK ARVIEVLVKA GDQVQAEQSL IVLESDKASM EIPSPASGVV ESVAIQLNAE VGTGDLILTL RTTGAQAQPT APAAAAAASP APAPLAPAAA GPQEVKVPDI GSAGKARVIE VLVKAGDQVQ AEQSLIVLES DKASMEIPSP AAGVVESVAV QLNAEVGTGD QILTLRVAGA APSGPRARGS PGQAAAAPGA APAPAPVGAP SRNGAKVHAG PAVRQLAREF GVELAAINST GPRGRILKED VQAYVKAMMQ KAKEAPAAGA ASGAGIPPIP PVDFAKYGEI EEVPMTRLMQ IGATNLHRSW LNVPHVTQFE SADITELEAF RVAQKAVAEK AGVKLTVLPL LLKACAYLLK ELPDFNSSLA PSGQALIRKK YVHIGFAVDT PDGLLVPVIR NVDQKSLLQL AAEAAELAEK ARSKKLGADA MQGACFTISS LGHIGGTAFT PIVNAPEVAI LGVSKASMQP VWDGKAFQPR LMLPLSLSYD HRVINGAAAA RFTKRLGDLL ADIRAILL //