ID A0A016UYH8_9BILA Unreviewed; 400 AA.
AC A0A016UYH8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000256|RuleBase:RU361139};
DE EC=1.2.4.1 {ECO:0000256|RuleBase:RU361139};
GN Name=Acey_s0024.g912 {ECO:0000313|EMBL:EYC19523.1};
GN Synonyms=Acey-pdha-1 {ECO:0000313|EMBL:EYC19523.1};
GN ORFNames=Y032_0024g912 {ECO:0000313|EMBL:EYC19523.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYC19523.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EYC19523.1}.
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DR EMBL; JARK01001360; EYC19523.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016UYH8; -.
DR Proteomes; UP000024635; 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:UP000024635};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU361139};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 64..354
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 400 AA; 44270 MW; 94315F1EDC2A3326 CRC64;
MSLLVKSFKA PAPILTAAIV ASQRRMASGG EVTFHTKGYK LHKLDSGPNE TVTLKREDAL
DYYRKMQLIR RMESAAGNLY KEKKIRGFCH LYSGQEACAV GMRSAMTEGD AVITAYRCHG
WTLLQGATVA EVLSELTGRI TGNVHGKGGS MHMYQKDFYG GNGIVGAQQP LGTGIAFAMK
YKKQKNVCLT LYGDGAANQG QLYESMNMAA LWNLPVLYVC ENNGFGMGTQ ADRASASTDY
YMRGDYVPGV WVDGMDVLAV RESIRWAKEY CNAGKGPLVI EMATYRYHGH SMSDPGTSYR
TREEIQEVRK TRDPITGFKD RIITSGLATE DDLKALDKDV RKEVDEAVKV ANTAELMPDE
GVYTDLYHNT EPQLIRGATM DVSHVQKYIH SADLMTSLKK
//
