ID A0A086H340_STRSC Unreviewed; 378 AA.
AC A0A086H340;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KFG02058.1};
GN ORFNames=IQ62_03655 {ECO:0000313|EMBL:KFG02058.1};
OS Streptomyces scabiei.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1930 {ECO:0000313|EMBL:KFG02058.1, ECO:0000313|Proteomes:UP000028722};
RN [1] {ECO:0000313|EMBL:KFG02058.1, ECO:0000313|Proteomes:UP000028722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4086 {ECO:0000313|EMBL:KFG02058.1,
RC ECO:0000313|Proteomes:UP000028722};
RA Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT "Genome sequencing of plant-pathogenic Streptomyces species.";
RL Submitted (JUL-2014) 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:KFG02058.1}.
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DR EMBL; JPPX01000041; KFG02058.1; -; Genomic_DNA.
DR RefSeq; WP_037689753.1; NZ_KL997396.1.
DR AlphaFoldDB; A0A086H340; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000028722; 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:KFG02058.1}.
FT DOMAIN 67..342
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 378 AA; 40840 MW; F5879B5582B33002 CRC64;
MTVMEQRGAY RPTPPPAWQP RTDPAPLLPD ATPYRVLGTD AAADADPALL RRLYAELVRG
RRYNTQATAL TKQGRLAVYP SSTGQEACEV AAALVLEERD WLFPSYRDTL AAVARGLDPV
QALTLLRGDW HTGYDPREHR VAPLCTPLAT QLPHAVGLAH AARLKGDDVV ALALVGDGGT
SEGDFHEALN FAAVWQAPVV FLVQNNGFAI SVPLAKQTAA PSLAHKAVGY GMPGRLVDGN
DAAAVHQVLA EAVAHARAGG GPTLVEAVTY RIDAHTNADD ATRYRGDAEV ETWRAHDPIA
LLEHELTERG LLDEEGVRAA RDAAETMAAD LRERMNQDPV LDPMDLFAHV YAEPTPQLRE
QEALLRAELA AEQEGAHR
//
