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Database: UniProt
Entry: A0A327WGG9_9ACTN
LinkDB: A0A327WGG9_9ACTN
Original site: A0A327WGG9_9ACTN 
ID   A0A327WGG9_9ACTN        Unreviewed;       395 AA.
AC   A0A327WGG9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Pyruvate dehydrogenase E1 component alpha subunit {ECO:0000313|EMBL:RAJ88691.1};
GN   ORFNames=K377_02147 {ECO:0000313|EMBL:RAJ88691.1};
OS   Streptomyces sp. PsTaAH-137.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1305830 {ECO:0000313|EMBL:RAJ88691.1, ECO:0000313|Proteomes:UP000249376};
RN   [1] {ECO:0000313|EMBL:RAJ88691.1, ECO:0000313|Proteomes:UP000249376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PsTaAH-137 {ECO:0000313|EMBL:RAJ88691.1,
RC   ECO:0000313|Proteomes:UP000249376};
RA   Currie C.;
RT   "Biomass-degrading enzyme discovery via genome sequencing of insect-
RT   associated Streptomyces.";
RL   Submitted (JUN-2018) 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:RAJ88691.1}.
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DR   EMBL; QLLY01000004; RAJ88691.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A327WGG9; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000249376; 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:RAJ88691.1}.
FT   DOMAIN          74..334
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   395 AA;  43378 MW;  443F180EC8E3A80C CRC64;
     MTVDSAASTG AARTPRKRTA ASKTAKKSPG RTAAAKGKSD LVQLLTPEGE RVKSTEYDTY
     VADITDDALR GLYRDMVMAR RFDAEAVTLQ RQGELGLWPS LLGQEAAQVG SARATRDDDY
     VFPTYREHGV AWCRGVEPEN LLGMFRGVNN GGWDPNTNNF HLYTIVIGSQ TLHATGYAMG
     IAKDGADSAV IAYFGDGASS QGDVAESFTF SAVYNAPVVF FCQNNQWAIS EPTEKQTRVP
     LYQRAQGFGF PGVRVDGNDV LACLAVTRWA LERARAGEGP TLVEAFTYRM GAHTTSDDPT
     KYRADEERVA WEAKDPILRL RAYLENHTDT GAEFFTDLET ESETLGRRVR EAVRGMQDPD
     RMAMFEHGYA DGHALVDEER AQFAAYQASF AEEGA
//
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