ID   A0A0Q9KDN2_9MICO        Unreviewed;       413 AA.
AC   A0A0Q9KDN2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Pyruvate dehydrogenase (Acetyl-transferring) E1 component subunit alpha {ECO:0000313|EMBL:KRE39463.1};
GN   ORFNames=ASG73_03865 {ECO:0000313|EMBL:KRE39463.1};
OS   Janibacter sp. Soil728.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Janibacter.
OX   NCBI_TaxID=1736393 {ECO:0000313|EMBL:KRE39463.1, ECO:0000313|Proteomes:UP000051572};
RN   [1] {ECO:0000313|EMBL:KRE39463.1, ECO:0000313|Proteomes:UP000051572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil728 {ECO:0000313|EMBL:KRE39463.1,
RC   ECO:0000313|Proteomes:UP000051572};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE39463.1, ECO:0000313|Proteomes:UP000051572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil728 {ECO:0000313|EMBL:KRE39463.1,
RC   ECO:0000313|Proteomes:UP000051572};
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:KRE39463.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LMRZ01000001; KRE39463.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q9KDN2; -.
DR   STRING; 1736393.ASG73_03865; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000051572; 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; IPR017596; PdhA/BkdA.
DR   InterPro; IPR029061; THDP-binding.
DR   NCBIfam; TIGR03181; PDH_E1_alph_x; 1.
DR   PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 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:KRE39463.1}.
FT   DOMAIN          84..373
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   413 AA;  45128 MW;  3A755A870A6379FD CRC64;
     MSDSDVAGHA GTRGRMAGAF EPSPEMGPTP PSQISGHFSD DNPEMVQFVD ADGNRLATNE
     TNAPYAQIVE DMTSEDARTI YRDLVLVRRI DAEGFALQRQ GELGLWPSLF GQEAAQVGAG
     RALRAQDYAF PGYREHGVAW CRGVDPVSLF GMFRGVNHGG WDSNENNFHL YTIVIGNQML
     HAVGYGMGIA ADGDMGTGDP ERDAAVMAFT GDGGTSQGDF NEALVFAAVT NAPVVFFVQN
     NQWAISEPND KQFIIPPYQR ARGFGFPGVL VDGNDPLASY AVAKDALDKA RSGQGPTLIE
     AYTYRMGAHT TSDDPTKYRS DAEVEIWKHK DPIKRMRGFM QERGHADPEF FAAVDAEADE
     VAARIRKACQ EMPDPELPTM FDNQYTEPHP LVEAEREEFL AYHAGFAEEG GQA
//