ID V6K3G6_STRRC Unreviewed; 901 AA.
AC V6K3G6;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=M878_33180 {ECO:0000313|EMBL:EST23499.1};
OS Streptomyces roseochromogenus subsp. oscitans DS 12.976.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352936 {ECO:0000313|EMBL:EST23499.1, ECO:0000313|Proteomes:UP000017984};
RN [1] {ECO:0000313|EMBL:EST23499.1, ECO:0000313|Proteomes:UP000017984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS 12.976 {ECO:0000313|EMBL:EST23499.1,
RC ECO:0000313|Proteomes:UP000017984};
RX PubMed=24407645;
RA Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces roseochromogenes subsp. oscitans DS
RT 12.976, Producer of the Aminocoumarin Antibiotic Clorobiocin.";
RL Genome Announc. 2:e01147-e01113(2014).
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};
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:EST23499.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AWQX01000283; EST23499.1; -; Genomic_DNA.
DR RefSeq; WP_023551327.1; NZ_CM002285.1.
DR AlphaFoldDB; V6K3G6; -.
DR STRING; 1352936.M878_33180; -.
DR PATRIC; fig|1352936.5.peg.6913; -.
DR HOGENOM; CLU_009154_2_0_11; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000017984; 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:EST23499.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017984};
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 901 AA; 98650 MW; 503E4045DE98A507 CRC64;
MTDPNAIQPS ALDQLPDRDP EETAEWQASL DAVAREAGPH RAAYLMRRTL ERAEAGGIAL
PKLLETDYVN TIPTSAEPGL PGDPEMEARI TAWNRWNAAA MVTRGSKHGV GGHIATFASA
AWLYETGFNH FFKGKEGDGS GDQLYIQGHA SPGVYARAFL DGRLNEHHLD NFRQEAGGNG
LPSYPHPRRL PWLWEFPTVS MGLGPLSAIY QARFNRYLTN RGIKDVSSSH VWAFLGDGEM
DEPESTAALA LASREGLDNL TFVINCNLQR LDGPVRANFK IVQELEAQFR GAGWNVVKTL
WGSAWDELFA LDTTGALVRR LREVPDAQIQ TYQTRDAAYI RADFFGKDPA LAEMAKLLSD
DKILECFHLS RGGHEARKVY AAYKAAVEHK GAPTVILAQT VKGHTLGDGF ASKNANHQMK
KLTVDEFKTM RDLLELPISD SQFIDGVVPY GHPGADSPEV RYLQERRAAL GGPAPARRTH
ALAPLPAPAE KTFASFDKGS GSQNVATTMA FVRLVKDLVR DKETGKRWVP IVPDEARTFG
MESLFPSLGI YSPKGQTYEP VDRDQLMYYK EAKNGQILNE GITEAGSMAD FIAASTAYAT
HGEAMIPFYI FYSMFGWQRT ADQMWQLGDQ LGRGFLVGAT AGRTTLTGEG LQHADGHSPV
IAATNPAALT YDPAFAYEIA VIVREGLRRM YGEAKPGEDQ NVFYYLTVYN EPLPQPAKPQ
GLGIDEGIVK GLYRFSTAES AGVNVAAANA PRIQLLGSGT AIHWAVEAQK LLAEEWGVAA
DVWSATSWSE LRRDAMEADA ALLRGEERVP YVRQALQGAE GPVLAVSDYM RQVPDQIAQW
VEQDYSSLGA DGFGLSDTRE AARRHFGVDA QSIVVAALAQ LAKRGEVKAT AVKEAREKYG
L
//
