ID D3TMY3_GLOMM Unreviewed; 403 AA.
AC D3TMY3;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000256|RuleBase:RU361139};
DE EC=1.2.4.1 {ECO:0000256|RuleBase:RU361139};
OS Glossina morsitans morsitans (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=37546 {ECO:0000313|EMBL:ADD19061.1};
RN [1] {ECO:0000313|EMBL:ADD19061.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland {ECO:0000313|EMBL:ADD19061.1};
RX PubMed=20353571; DOI=10.1186/1471-2164-11-213;
RA Alves-Silva J., Ribeiro J.M., Van Den Abbeele J., Attardo G., Hao Z.,
RA Haines L.R., Soares M.B., Berriman M., Aksoy S., Lehane M.J.;
RT "An insight into the sialome of Glossina morsitans morsitans.";
RL BMC Genomics 11:213-213(2010).
RN [2] {ECO:0000313|EMBL:ADD19061.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland {ECO:0000313|EMBL:ADD19061.1};
RG International Glossina Genome Initiative;
RA da Silva J., Ribeiro J.M.C., Abbeele J.V., Attardo G., Hao Z., Haines L.R.,
RA Soares M.B., Berriman M., Aksoy S., Lehane M.J.;
RL Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00043719,
CC 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; EZ422785; ADD19061.1; -; mRNA.
DR AlphaFoldDB; D3TMY3; -.
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 2: Evidence at transcript level;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU361139};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|RuleBase:RU361139};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU361139};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 75..366
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 403 AA; 44536 MW; 15BAFB6F92D3BF0A CRC64;
MLRQLSRAAD LPVVLRQLQK STARNGAAAA AQQTNNYATE ATIQIQRPFK LHRLDQGPET
SVKLTKEEAL LYYTQMQVIR RIETSAGNLY KEKIIRGFCH LYSGQEACAV GMKSAMTDVD
NIISAYRVHG WTYLMGVPPL GVLAELTGRQ KGSSRGKGGS MHMYGRNFYG GNGIVGAQVP
LGAGVALACQ YKGNGGMCYA LYGDGASNQG QVFEAYNMAY LWRLPVIFVC ENNNYGMGTS
AERSSCNTDY YTRGDVIPGI WVDGMDVLAV RSASLFAREY ATKKGPIVLE TNTYRYSGHS
MSDPGTSYRT REEIQEVRSK RDPISSFKEL CIEHGLISAD EVKVIDNKVR KEVDEATAQA
KADTELPLQG LWTDVYSDCL EPKIRGAVDY DIDHIQENKG INH
//
