ID R4FK33_RHOPR Unreviewed; 386 AA.
AC R4FK33;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000256|RuleBase:RU361139};
DE EC=1.2.4.1 {ECO:0000256|RuleBase:RU361139};
OS Rhodnius prolixus (Triatomid bug).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX NCBI_TaxID=13249 {ECO:0000313|EMBL:JAA75457.1};
RN [1] {ECO:0000313|EMBL:JAA75457.1}
RP NUCLEOTIDE SEQUENCE.
RA Ribeiro J.M.C., Genta F.A., Sorgine M.H.F., Paiva-Silva G.O.,
RA Majerowicz D., Medeiros M., Koerich L., Terra W.R., Ferreira C.,
RA Pimentel A.C., Bisch P.M., Diniz M.M.P., Nascimento R., Salmon D.,
RA Silber A.M., Alves M., Oliveira M.F., Gondim K.C., Silva Neto M.A.C.,
RA Atella G.C., Araujo H., Dias F.S., Polycarpo C.R., Fampa P., Melo A.C.,
RA Tanaka A.S., Balczun C., Oliveira J.H.M., Goncalves R., Lazoski C.,
RA Pereira M.A., Rivera-Pomar R., Diambra L., Schaub G.A., Garcia E.S.,
RA Azambuja P., Braz G.R.C., Oliveira P.L.;
RT "An insight into the transcriptome of the digestive tract of the blood
RT sucking bug, Rhodnius prolixus.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000015103}
RP NUCLEOTIDE SEQUENCE.
RA Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:RPRC009715-PA}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (MAY-2015) to UniProtKB.
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; ACPB03009632; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; GAHY01002053; JAA75457.1; -; mRNA.
DR AlphaFoldDB; R4FK33; -.
DR STRING; 13249.R4FK33; -.
DR EnsemblMetazoa; RPRC009715-RA; RPRC009715-PA; RPRC009715.
DR VEuPathDB; VectorBase:RPRC009715; -.
DR eggNOG; KOG0225; Eukaryota.
DR HOGENOM; CLU_029393_5_2_1; -.
DR InParanoid; R4FK33; -.
DR OMA; EPYRRMW; -.
DR OrthoDB; 166915at2759; -.
DR Proteomes; UP000015103; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000015103};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU361139};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 58..352
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 386 AA; 42832 MW; 853E625BB4253F47 CRC64;
MNVTKKINVP QLIFKYSKRL VSEANFTIQE PFRLHRLEKG PLTKVTLTKQ DALTYYKKMS
TIRRVENTSA NLYMEKVIRG FCHLYAGQEA VAVGIQATMR PDDCLITAYR AHGWVLLMGG
SPEQILGELC GRVIGCSRGK GGSMHTYAKN FFGGNGIVGA QIPMGTGIGL MMKLTGKPNV
SFALYGDGAA NQGQVFEAYN LAKLWNLPVI FVCENNKYGM GTSAERASAV PEFYTRGDYI
PGIQVDGMDV LATREASLFA IAHCISNRGP ILLEMVTYRY YGHSMSDPGT SYRSRNEVQD
IRKNKDPITL FKDKILGANL VSEEEIKQLD NETKKIIEEA TAKVRAAPVP GPEELVADVY
KKPVTPNVRG VNPWRTLKHI QITKPK
//
