ID Q8SQM8_ENCCU Unreviewed; 349 AA.
AC Q8SQM8;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE SubName: Full=PYRUVATE DEHYDROGENASE E1 COMPONENT ALPHA SUBUNIT {ECO:0000313|EMBL:CAD27078.1};
GN OrderedLocusNames=ECU09_1040 {ECO:0000313|EMBL:CAD27078.1};
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813 {ECO:0000313|EMBL:CAD27078.1, ECO:0000313|Proteomes:UP000000819};
RN [1] {ECO:0000313|EMBL:CAD27078.1, ECO:0000313|Proteomes:UP000000819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1 {ECO:0000313|EMBL:CAD27078.1,
RC ECO:0000313|Proteomes:UP000000819};
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR EMBL; AL590451; CAD27078.1; -; Genomic_DNA.
DR RefSeq; XP_955659.1; XM_950566.1.
DR AlphaFoldDB; Q8SQM8; -.
DR STRING; 284813.Q8SQM8; -.
DR VEuPathDB; MicrosporidiaDB:ECU09_1040; -.
DR HOGENOM; CLU_029393_5_2_1; -.
DR InParanoid; Q8SQM8; -.
DR OMA; NWSVACD; -.
DR OrthoDB; 166915at2759; -.
DR Proteomes; UP000000819; Chromosome IX.
DR GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; 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; IPR029061; THDP-binding.
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 Pyruvate {ECO:0000313|EMBL:CAD27078.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000819}.
FT DOMAIN 45..335
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 349 AA; 39199 MW; EF61312BB362F7DA CRC64;
MEGERYVSCD VQEILDSIQA HRIGKEEIGI VHRIGVDKAV YIYKQMMRMR CMDEAMDREY
KRKNIRGFCH LSIGQEGIYA ALEYAMDGDV AVSSYRCHGI AYVTGCSILE IMGEVLGRQA
GVCKGKGGSM HLYNKSFFGG HGIVGAQIPL GLGMAYALEY NRRMGWSQGG KVCYAFYGDG
AANQGQVWES FNMAMVWRLP IVFVCENNGY GMWTPASSVS ADTDFYLRGG AIPGIRIGHG
NIFGLMSVLK YARKYSVENG PIIVQIDTYR FCTHSAADER ESYRSREEVD AEKKRDCMED
VGRRLLAFYS EEELDALRSS ILAEVERDVD AARKSRPTEE DELCRDILL
//
