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Database: UniProt
Entry: F2SVI8_TRIRC
LinkDB: F2SVI8_TRIRC
Original site: F2SVI8_TRIRC 
ID   F2SVI8_TRIRC            Unreviewed;       431 AA.
AC   F2SVI8;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 2.
DT   24-JAN-2024, entry version 39.
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=TERG_06560 {ECO:0000313|EMBL:EGD90332.2};
OS   Trichophyton rubrum (strain ATCC MYA-4607 / CBS 118892) (Athlete's foot
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559305 {ECO:0000313|EMBL:EGD90332.2, ECO:0000313|Proteomes:UP000008864};
RN   [1] {ECO:0000313|Proteomes:UP000008864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4607 / CBS 118892 {ECO:0000313|Proteomes:UP000008864};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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; GG700655; EGD90332.2; -; Genomic_DNA.
DR   AlphaFoldDB; F2SVI8; -.
DR   STRING; 559305.F2SVI8; -.
DR   InParanoid; F2SVI8; -.
DR   OMA; LGYEMPC; -.
DR   OrthoDB; 166915at2759; -.
DR   Proteomes; UP000008864; 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:UP000008864};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU361139}.
FT   DOMAIN          106..400
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   431 AA;  48175 MW;  ADB9ACAAE5F09699 CRC64;
     MFSRLIRARG VAQVGRQPST QLFRRSVTTD AASAHAEDIP VVRLPGLPIE RIYAGRKSAN
     HSFARLQEDD KPFSVKLSDE SFETYELDPP PYTLKTTKKE LKQMYYDMVS IRRMEMAADR
     LYKEKKIRGF CHLSTGQEAV ATGIEHAITP DDKLITAYRC HGFAMMRGGT VRSIIGELLG
     RREGIAYGKG GSMHMFAKNF FGGNGIVGAQ VPVGAGLAFA QQYNGEANTT VCLYGDGASN
     QGQVFEAFNM AKLWNLPVMF GCENNKYGMG TAANRSSALT DYYKRGQYIP GIKINGMDVL
     AIKAAVQYGR EYTVSGQGPL VFEYVTYRYG GHSMSDPGTT YRTREEIQRM RSTNDPIAGL
     KQKLLDWNIT SEDELKAIDK DARSMVDEEV AIAEKMPVPD ATPRILFEDI YVRGSEPKWM
     RGRTADETFY Y
//
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