ID ODPA_PORPU Reviewed; 344 AA. AC P51267; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 02-SEP-2026, entry version 84. DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha; DE EC=1.2.4.1; GN Name=pdhA; Synonyms=odpA; OS Porphyra purpurea (Red seaweed) (Ulva purpurea). OG Plastid; Chloroplast. OC Eukaryota; Rhodophyta; Bangiophyceae; Bangiales; Bangiaceae; Porphyra. OX NCBI_TaxID=2787; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Avonport; RX DOI=10.1007/BF02669187; RA Reith M.E., Munholland J.; RT "Complete nucleotide sequence of the Porphyra purpurea chloroplast RT genome."; RL Plant Mol. Biol. Rep. 13:333-335(1995). 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) (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N(6)-[(R)-lipoyl]-L-lysyl-[protein] + pyruvate + H(+) = N(6)- CC [(R)-S(8)-acetyldihydrolipoyl]-L-lysyl-[protein] + CO2; CC Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10474, Rhea:RHEA-COMP:10478, CC ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, CC ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000250|UniProtKB:P08559}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P08559}; CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast. 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; U38804; AAC08153.1; -; Genomic_DNA. DR PIR; S73188; S73188. DR RefSeq; NP_053877.1; NC_000925.1. DR AlphaFoldDB; P51267; -. DR SMR; P51267; -. DR GeneID; 809896; -. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC. DR GO; GO:0006086; P:pyruvate decarboxylation to acetyl-CoA; IEA:InterPro. DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1. DR FunFam; 3.40.50.970:FF:000013; Pyruvate dehydrogenase E1 component subunit alpha; 1. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR001017; DH_E1. DR InterPro; IPR050642; PDH_E1_Alpha_Subunit. DR InterPro; IPR017597; Pyrv_DH_E1_asu_subgrp-y. DR InterPro; IPR029061; THDP-binding. DR NCBIfam; TIGR03182; PDH_E1_alph_y; 1. DR PANTHER; PTHR11516:SF60; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT ALPHA; 1. DR PANTHER; PTHR11516; PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT BACTERIAL AND ORGANELLAR; 1. DR Pfam; PF00676; E1_dh; 1. DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1. PE 3: Inferred from homology; KW Chloroplast; Magnesium; Metal-binding; Oxidoreductase; Plastid; Pyruvate; KW Thiamine pyrophosphate. FT CHAIN 1..344 FT /note="Pyruvate dehydrogenase E1 component subunit alpha" FT /id="PRO_0000162215" FT BINDING 55 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000250|UniProtKB:P08559" FT BINDING 81 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000250|UniProtKB:P08559" FT BINDING 81 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_note="ligand shared with beta subunit" FT /evidence="ECO:0000250|UniProtKB:P08559" FT BINDING 82 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000250|UniProtKB:P08559" FT BINDING 82 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_note="ligand shared with beta subunit" FT /evidence="ECO:0000250|UniProtKB:P08559" FT BINDING 130 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000250|UniProtKB:P08559" FT BINDING 130 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_note="ligand shared with beta subunit" FT /evidence="ECO:0000250|UniProtKB:P08559" FT BINDING 132 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000250|UniProtKB:P08559" FT BINDING 132 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_note="ligand shared with beta subunit" FT /evidence="ECO:0000250|UniProtKB:P08559" FT BINDING 168 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P08559" FT BINDING 168 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000250|UniProtKB:P08559" FT BINDING 168 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_note="ligand shared with beta subunit" FT /evidence="ECO:0000250|UniProtKB:P08559" FT BINDING 169 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000250|UniProtKB:P08559" FT BINDING 169 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_note="ligand shared with beta subunit" FT /evidence="ECO:0000250|UniProtKB:P08559" FT BINDING 197 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P08559" FT BINDING 197 FT /ligand="pyruvate" FT /ligand_id="ChEBI:CHEBI:15361" FT /evidence="ECO:0000250|UniProtKB:P08559" FT BINDING 197 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_note="ligand shared with beta subunit" FT /evidence="ECO:0000250|UniProtKB:P08559" FT BINDING 266 FT /ligand="thiamine diphosphate" FT /ligand_id="ChEBI:CHEBI:58937" FT /ligand_note="ligand shared with beta subunit" FT /evidence="ECO:0000250|UniProtKB:P08559" SQ SEQUENCE 344 AA; 38507 MW; 799BD9AFA06FF455 CRC64; MSYPKKVELP LTNCNQINLT KHKLLVLYED MLLGRNFEDM CAQMYYKGKM FGFVHLYNGQ EAVSTGVIKL LDSKDYVCST YRDHVHALSK GVPSQNVMAE LFGKETGCSR GRGGSMHIFS APHNFLGGFA FIAEGIPVAT GAAFQSIYRQ QVLKEPGELR VTACFFGDGT TNNGQFFECL NMAVLWKLPI IFVVENNQWA IGMAHHRSSS IPEIHKKAEA FGLPGIEVDG MDVLAVRQVA EKAVERARQG QGPTLIEALT YRFRGHSLAD PDELRSRQEK EAWVARDPIK KLKKHILDNQ IASSDELNDI QSSVKIDLEQ SVEFAMSSPE PNISELKRYL FADN //