ID A0A0D0N4K1_KITGR Unreviewed; 383 AA.
AC A0A0D0N4K1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Pyruvate dehydrogenase {ECO:0000313|EMBL:KIQ63050.1};
GN ORFNames=TR51_30045 {ECO:0000313|EMBL:KIQ63050.1};
OS Kitasatospora griseola (Streptomyces griseolosporeus).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=2064 {ECO:0000313|EMBL:KIQ63050.1, ECO:0000313|Proteomes:UP000032066};
RN [1] {ECO:0000313|EMBL:KIQ63050.1, ECO:0000313|Proteomes:UP000032066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MF730-N6 {ECO:0000313|EMBL:KIQ63050.1,
RC ECO:0000313|Proteomes:UP000032066};
RA Arens J.C., Haltli B., Kerr R.G.;
RT "Draft genome sequence of Kitasatospora griseola MF730-N6, a bafilomycin,
RT terpentecin and satosporin producer.";
RL Submitted (FEB-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:KIQ63050.1}.
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DR EMBL; JXZB01000004; KIQ63050.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0N4K1; -.
DR STRING; 2064.TR51_30045; -.
DR PATRIC; fig|2064.6.peg.6374; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000032066; 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:KIQ63050.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000032066}.
FT DOMAIN 64..332
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 383 AA; 41063 MW; 2E3BC5FC8A04A78E CRC64;
MTVLDHRDQA DPGVVPGWLP GATAPRTDPV PLLPDDEPLR VLGTPAADKA DPALLRELYR
RLVAGRRYNQ QATTLTKQGR LAVYPASTGQ EACQIAAALA LRSDDWLFPS YRDTLAVVAR
GVDPLEALTL LRGNAHTGYD PRATRTAPLC TPLATQVPHA VGLAHAARLA GDDTVALALL
GDGGTSEGDF HEGLNFAAVL HAPVVFLVQN NGYAISVPLT RQSAAPTLAH KAVGYGMPGR
LVDGNDAAAV HQVLTEALER ARSGGGPTLV EALTYRVEAH TNADDATRYR QAEEVTAWQA
HDPIRLLEDA LRERDLLDDR LVAEAGEEAE AMAARMRAEF HADPDLDPMS LFAHVYAEPT
QQLREQAAQL AAELAAEAEV HTR
//
