ID   A0A1A9UKA5_GLOAU        Unreviewed;       886 AA.
AC   A0A1A9UKA5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00017172};
DE            EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281};
OS   Glossina austeni (Savannah tsetse fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC   Glossinidae; Glossina.
OX   NCBI_TaxID=7395 {ECO:0000313|EnsemblMetazoa:GAUT007483-PA, ECO:0000313|Proteomes:UP000078200};
RN   [1] {ECO:0000313|Proteomes:UP000078200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TTRI {ECO:0000313|Proteomes:UP000078200};
RA   Aksoy S., Warren W., Wilson R.K.;
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:GAUT007483-PA}
RP   IDENTIFICATION.
RC   STRAIN=TTRI {ECO:0000313|EnsemblMetazoa:GAUT007483-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
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|ARBA:ARBA00043719};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   AlphaFoldDB; A0A1A9UKA5; -.
DR   STRING; 7395.A0A1A9UKA5; -.
DR   EnsemblMetazoa; GAUT007483-RA; GAUT007483-PA; GAUT007483.
DR   VEuPathDB; VectorBase:GAUT007483; -.
DR   OrthoDB; 3638585at2759; -.
DR   Proteomes; UP000078200; Unassembled WGS sequence.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   CDD; cd02017; TPP_E1_EcPDC_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR035807; PDC_E1_N.
DR   InterPro; IPR004660; PDH_E1.
DR   InterPro; IPR041621; PDH_E1_M.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005474; Transketolase_N.
DR   NCBIfam; TIGR00759; aceE; 1.
DR   PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   PANTHER; PTHR43825:SF3; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR   Pfam; PF17831; PDH_E1_M; 1.
DR   Pfam; PF00456; Transketolase_N; 2.
DR   PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          103..294
FT                   /note="Transketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00456"
FT   DOMAIN          359..444
FT                   /note="Transketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00456"
FT   DOMAIN          488..699
FT                   /note="Pyruvate dehydrogenase E1 component middle"
FT                   /evidence="ECO:0000259|Pfam:PF17831"
SQ   SEQUENCE   886 AA;  101474 MW;  F576439169F0367F CRC64;
     MSKHLYYDID SIETNEWIES IRSVIKSDGI LRAQYLIDRI LQETKKNCKN KTIYNQNYIN
     SISSEEEPKY PGNLKLEHRI RSVIRWNAVM MVLKASKKNL ELGGHISSFQ SAATIYEVCF
     NHFFRGPKSE DGGDLIYFQG HISPGIYSRA FLEGRLTKKN LDNFRQETYG YGLSSYPHPK
     LMPNFWQFPT VSMGLGAISG IYQAKFLKYL HHRKIKNTEK KTVYVFLGDG EMDEPESKGA
     INIAVREKLD NLIFIVNCNL QRLDGPVYGN GKIINELTDF FQGAGWEVIR VIWGSKWDVL
     LKKDKSGKLI QLMNETVDGD YQNLKSKNGA YIRKNFFGKF FETEQLVKDM TDDEIWNLNR
     GGHDPKKIYA ALKKAKNIQN KPAIILVHTV KGYGMGDLAE GKNIAHQVKN MNETSIKKFR
     DRFNLYDIKD NQLNVMPYIS FQKKSKEYEY LHNCRKKLHG YLPNRTHQLG SMNNLPSLED
     FTSLLKEQKK NISTTIAFVR ILNILLKNQF IAKYLVPIIA DEARTFGMEG LFRQIGIYNQ
     HGQKYIPQDQ EQLAYYKEEK TGQILQEGIN ELGATASWIS AATSYSTNQV TMIPFYIYYS
     MFGFQRIGDL IWSASDQQAR GFLIGATSGR TTLNGEGLQH ADGHSHIQSL VIPNCISYNP
     TYSYELAVII QNGLHRMYGK NPENIFYYIT TLNENYHMPA IPRGAEEGIC KGIYKLESRL
     SGTKKVQLIG SGSILRQVRI AAKVLSEDYN ISVDVYSATS FTEIARNGQD CMRWNTLHPT
     KQPRIPYISQ IMHSAPIVVS TDYIKLFAEQ IRNFLPSNIF KVLGTDGFGR SDSRENLRKH
     FEINSEYIIV NALSALYEEK SITIEVVTQA IKNFNIDADK INPRLV
//