ID F8JTM4_STREN Unreviewed; 356 AA.
AC F8JTM4; G8WV27;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=pdhA {ECO:0000256|RuleBase:RU361139};
GN OrderedLocusNames=SCATT_44200 {ECO:0000313|EMBL:AEW96791.1};
OS Streptantibioticus cattleyicolor (strain ATCC 35852 / DSM 46488 / JCM 4925
OS / NBRC 14057 / NRRL 8057) (Streptomyces cattleya).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptantibioticus.
OX NCBI_TaxID=1003195 {ECO:0000313|EMBL:AEW96791.1, ECO:0000313|Proteomes:UP000007842};
RN [1] {ECO:0000313|Proteomes:UP000007842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057
RC {ECO:0000313|Proteomes:UP000007842};
RA Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.;
RT "Complete genome sequence of Streptomyces cattleya strain DSM 46488.";
RL Submitted (DEC-2011) 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|RuleBase:RU361139};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|RuleBase:RU361139};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|RuleBase:RU361139}.
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DR EMBL; CP003219; AEW96791.1; -; Genomic_DNA.
DR RefSeq; WP_014145137.1; NC_017586.1.
DR AlphaFoldDB; F8JTM4; -.
DR STRING; 1003195.SCATT_44200; -.
DR KEGG; scy:SCATT_44200; -.
DR PATRIC; fig|1003195.11.peg.5868; -.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_029393_5_0_11; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000007842; Chromosome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:InterPro.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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:SF72; DEHYDROGENASE-RELATED; 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:UP000007842};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU361139}.
FT DOMAIN 30..327
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 356 AA; 38315 MW; 89E35363AEDD1553 CRC64;
MGGRTRRGTR AEVVRSGGSY DPEDLIECAR RMLLVRRFEE RAAQAYTQAR VGGYCHLNLG
EEATVVGLTA ALEPGDYLFT NYREHGYALG RGIPAGRIMA ELYGRSTGVS KGWGGSMHMF
DAQARLMGGY GIVGGQLPLA TGAALAISYR GGAEVVMCQM GDGTTNIGAF HESLNIAALW
DLPVVFAVVN NQLGMGTSVQ ESSAEPELHR RAAAYRINGV RVDGTDVLAV REAAREAVRL
AREEHRPTLL ETVSHRLRGH SVVDPARYRD PEEAARAATA DPLPALRARL AADGALDDAG
WEAMDAAVRQ EVARAAEFAE NSPHPAVETL FDHTYATPVP NSEPRLPADA LFPQPL
//
