ID   A0A0S9Q7D3_9ACTN        Unreviewed;       334 AA.
AC   A0A0S9Q7D3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Pyruvate dehydrogenase (Acetyl-transferring) E1 component subunit alpha {ECO:0000313|EMBL:KQP65723.1};
GN   ORFNames=ASF47_08255 {ECO:0000313|EMBL:KQP65723.1};
OS   Nocardioides sp. Leaf285.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Nocardioides.
OX   NCBI_TaxID=1736322 {ECO:0000313|EMBL:KQP65723.1, ECO:0000313|Proteomes:UP000051495};
RN   [1] {ECO:0000313|EMBL:KQP65723.1, ECO:0000313|Proteomes:UP000051495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf285 {ECO:0000313|EMBL:KQP65723.1,
RC   ECO:0000313|Proteomes:UP000051495};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQP65723.1, ECO:0000313|Proteomes:UP000051495}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf285 {ECO:0000313|EMBL:KQP65723.1,
RC   ECO:0000313|Proteomes:UP000051495};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KQP65723.1}.
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DR   EMBL; LMNH01000002; KQP65723.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0S9Q7D3; -.
DR   Proteomes; UP000051495; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; 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; IPR029061; THDP-binding.
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   Pyruvate {ECO:0000313|EMBL:KQP65723.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051495}.
FT   DOMAIN          28..323
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   334 AA;  35350 MW;  E0F61E347D62ADB7 CRC64;
     MHICAKEPPV TSAPLADAGR ARHALLTMWT IRRFEEAVDD LFARGLMHGT MHLSIGQEAS
     ATGACMALRS DDAITSTHRG HGHCIGKGAD LTRMMAELLA KETGYCRGRG GSMHIADVAT
     GNLGANGIVA GGIPIATGAA LAYQLRGEDR VVACFFGDGA ANEGAFHEAV NLAAIWKLPV
     VFICENNKYG MSFSTEKSMA VAHVADRASA YGIPGVTVDG NDVEAVHAAV ADAVARARSG
     AGPTLVENVT YRWKGHSKSD KNLYRTKEEI AEWRALDPIV RFEAVVQERG LLDEAAVQAV
     RDEAMQAMRE AVRAANAAPD ADPSDLLDAV FAPA
//