ID A0A1D7YGV3_9ACTN Unreviewed; 900 AA.
AC A0A1D7YGV3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00017172, ECO:0000256|PIRNR:PIRNR000156};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281, ECO:0000256|PIRNR:PIRNR000156};
GN ORFNames=BFF78_30265 {ECO:0000313|EMBL:AOR34766.1};
OS Streptomyces fodineus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1904616 {ECO:0000313|EMBL:AOR34766.1, ECO:0000313|Proteomes:UP000094960};
RN [1] {ECO:0000313|Proteomes:UP000094960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW1S1 {ECO:0000313|Proteomes:UP000094960};
RA Kim M.-K., Kim S.B.;
RT "Streptomyces puniciscabiei strain:TW1S1 Genome sequencing and assembly.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex, that
CC catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
CC {ECO:0000256|PIRNR:PIRNR000156}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC Evidence={ECO:0000256|ARBA:ARBA00043719,
CC ECO:0000256|PIRNR:PIRNR000156};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000156-1};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|PIRNR:PIRNR000156};
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DR EMBL; CP017248; AOR34766.1; -; Genomic_DNA.
DR RefSeq; WP_069781312.1; NZ_CP017248.1.
DR AlphaFoldDB; A0A1D7YGV3; -.
DR KEGG; spun:BFF78_30265; -.
DR Proteomes; UP000094960; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd02017; TPP_E1_EcPDC_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR035807; PDC_E1_N.
DR InterPro; IPR004660; PDH_E1.
DR InterPro; IPR041621; PDH_E1_M.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00759; aceE; 1.
DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF3; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR Pfam; PF17831; PDH_E1_M; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000156-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000156-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000156};
KW Pyruvate {ECO:0000256|PIRNR:PIRNR000156, ECO:0000313|EMBL:AOR34766.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 147..299
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 487..712
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 237
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 900 AA; 98566 MW; D0DC5C65F0927F34 CRC64;
MTDPNAIQPS ALDQLPDRDP EETAEWQASL DAVAREAGPH RAAYLMRRTL ERAEAGGIAL
PKLLETDYVN TIPTAAEPAL PGDPEMEARI TAWNRWNAAA MVTRGSKYGV GGHIATFASA
AWLYETGFNH FFKGKEGDGS GDQLYIQGHA SPGIYARAFL DGRLNEAHLD NFRQEAGGNG
LPSYPHPRRL PWLWEFPTVS MGLGPLSAIY QARFNRYLTN RGIKDVSASH VWAFLGDGEM
DEPESTAALA LAAREELDNL TFVINCNLQR LDGPVRANFK IVQELEAQFR GAGWNVVKTL
WGSAWDELFA LDTTGALVRR LREVPDAQIQ TYQTRDAAYI RADFFGKDPA LAEMAKLLGD
DKILECFHLS RGGHEARKVY AAYKAAVEHK GAPTVILAQT VKGHTLGEGF ASKNANHQMK
KLTVDEFKTM RDLLGLPIKD SDFADGQVPY GHPGADSPEV RYLQERRAAL GGPAPARRTH
ALAPLPAPAE KAFASFDKGS GSQNVATTMA FVRLVKDLVR DKETGRRWVP IVPDEARTFG
MESLFPSLGI YSPKGQTYEP VDRDQLMYYK EAKNGQILNE GITEAGSMAD FIAASSSYAT
HGEAMIPFYI FYSMFGWQRT ADQMWQLGDQ LGRGFLVGAT AGRTTLTGEG LQHADGHSPV
IAATNPAALT YDPAFAYEIA VIVREGLRRM YGEAKPGEDQ NVFYYLTVYN EPLPQPAKPA
GLGIDEGIVK GLYRFNTVES AGLSPAANAP RIQLLGSGTA IHWALQAQKL LAEEWGVAAD
VWSATSWSEL RRDAMEADAA LLRGEERVPY VRQALQGAEG PVLAVSDYMR QVPDQIAQWV
EQDWSSLGAD GFGLSDTREA ARRHFGVDAE SIVVAALAQL AKRGEVKATA VKEARERYGL
//
