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Database: UniProt
Entry: A6QVF3_AJECN
LinkDB: A6QVF3_AJECN
Original site: A6QVF3_AJECN 
ID   A6QVF3_AJECN            Unreviewed;       405 AA.
AC   A6QVF3;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 71.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000256|RuleBase:RU361139};
DE            EC=1.2.4.1 {ECO:0000256|RuleBase:RU361139};
GN   ORFNames=HCAG_01360 {ECO:0000313|EMBL:EDN03495.1};
OS   Ajellomyces capsulatus (strain NAm1 / WU24) (Darling's disease fungus)
OS   (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=2059318 {ECO:0000313|EMBL:EDN03495.1, ECO:0000313|Proteomes:UP000009297};
RN   [1] {ECO:0000313|Proteomes:UP000009297}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NAm1 / WU24 {ECO:0000313|Proteomes:UP000009297};
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2).
CC       {ECO:0000256|RuleBase:RU361139}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC         acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC         Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC         Evidence={ECO:0000256|RuleBase:RU361139};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964,
CC         ECO:0000256|RuleBase:RU361139};
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DR   EMBL; CH476655; EDN03495.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6QVF3; -.
DR   STRING; 339724.A6QVF3; -.
DR   VEuPathDB; FungiDB:HCAG_01360; -.
DR   HOGENOM; CLU_029393_5_2_1; -.
DR   OMA; HGIVGGQ; -.
DR   OrthoDB; 166915at2759; -.
DR   Proteomes; UP000009297; Unassembled WGS sequence.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:InterPro.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006086; P:acetyl-CoA biosynthetic process from pyruvate; IEA:InterPro.
DR   CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR001017; DH_E1.
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   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361139};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU361139};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009297};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU361139}.
FT   DOMAIN          81..373
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   405 AA;  45191 MW;  6B31B5638E019C43 CRC64;
     MLSRITRVRQ VAPLCRKAFV PVVRRSVTTD AASAHAEAIP AEEDKPFTVK LSDESFETYE
     LDPPPYTLET TKQELKQMYR DMVSIRRMEM AADRLYKEKK IRGFCHLSTG QEAVATGIEH
     AITKDDKLIT AYRCHGFALL RGGTVKSIIG ELLGRREGIA YGKGGSMHMF AKNFYGGNGI
     VGAQVPVGAG LAFSQQYNDE KTTTIALYGD GASNQGQVFE AFNMAKLWNL PCIFGCENNK
     YGMGTAASRA AALTDYYKRG QYIPGLKING MDVLAIKAAV QYGREYTTSG KGPLVFEYVT
     YRYGGHSMSD PGTTYRTREE IQRMRSTNDP IAGLKQKLLD WGVTSEEELK AIDKDARKYV
     DDEVAEAELM TEPDATPRIL FEDTYVRGSE PAWTRGRTVD ETFYY
//
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