ID A0A0L0K9V5_9ACTN Unreviewed; 371 AA.
AC A0A0L0K9V5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KND34563.1};
GN ORFNames=IQ63_16015 {ECO:0000313|EMBL:KND34563.1};
OS Streptomyces acidiscabies.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=42234 {ECO:0000313|EMBL:KND34563.1, ECO:0000313|Proteomes:UP000037151};
RN [1] {ECO:0000313|Proteomes:UP000037151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
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:KND34563.1}.
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DR EMBL; JPPY01000108; KND34563.1; -; Genomic_DNA.
DR RefSeq; WP_050371266.1; NZ_KQ257820.1.
DR AlphaFoldDB; A0A0L0K9V5; -.
DR PATRIC; fig|42234.21.peg.3296; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000037151; 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:KND34563.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037151}.
FT DOMAIN 62..332
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 371 AA; 40127 MW; 90317138208E32C9 CRC64;
MTVMEQRGAY RPSPPPAWQP RMDPAPLLPD AEPYRVLGTE KPVDPELLLR LHAQLVRGRR
YNAQATALTK QGRLAVYPSS TGQEACEIAA ALAIEDRDWL FPSYRDTLAV VARGVDPVEA
LTLLRGDWHT GYDPYAHRVA PLCTPLATQL PHAVGLAHAA RLKGDDVVAL ALVGDGGTSE
GDFHEALNFA AVWQAPVVFL VQNNGFAISV PLAKQTAAPS LAHKAVGYGM PGRLVDGNDV
LAVHEVLTDA VRHARAGGGP TLIEAVTYRV EAHTNADDAT RYRGDAEVQA WREHDPIVLV
ERELTARGLL DDAHAQKVHD DAEAMAADLR ARMNQDAALD PDDLFAHVYA APTPQLREQQ
ALLHAEMEAG A
//
