ID A0A191UWM7_9ACTN Unreviewed; 900 AA.
AC A0A191UWM7;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=GCM10010220_28560 {ECO:0000313|EMBL:GGR74515.1},
GN Spa2297_09025 {ECO:0000313|EMBL:ANJ07134.1};
OS Streptomyces parvulus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=146923 {ECO:0000313|EMBL:ANJ07134.1, ECO:0000313|Proteomes:UP000078468};
RN [1] {ECO:0000313|EMBL:ANJ07134.1, ECO:0000313|Proteomes:UP000078468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2297 {ECO:0000313|EMBL:ANJ07134.1,
RC ECO:0000313|Proteomes:UP000078468};
RA Nishizawa T., Miura T., Harada C., Guo Y., Narisawa K., Ohta H.,
RA Takahashi H., Shirai M.;
RT "Non-Contiguous Finished Genome Sequence of Streptomyces parvulus 2297
RT Integrated Site-Specifically with Actinophage R4.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GGR74515.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 4068 {ECO:0000313|EMBL:GGR74515.1};
RX PubMed=30832757;
RA Wu L., Ma J.;
RT "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT project: providing services to taxonomists for standard genome sequencing
RT and annotation.";
RL Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN [3] {ECO:0000313|EMBL:GGR74515.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 4068 {ECO:0000313|EMBL:GGR74515.1};
RA Sun Q., Ohkuma M.;
RL Submitted (DEC-2022) 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; CP015866; ANJ07134.1; -; Genomic_DNA.
DR EMBL; BMRX01000006; GGR74515.1; -; Genomic_DNA.
DR RefSeq; WP_064727518.1; NZ_JAIWPL010000001.1.
DR AlphaFoldDB; A0A191UWM7; -.
DR KEGG; spav:Spa2297_09025; -.
DR Proteomes; UP000078468; Chromosome.
DR Proteomes; UP000645274; Unassembled WGS sequence.
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:ANJ07134.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 147..300
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 487..713
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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; 98746 MW; AC064719AA121967 CRC64;
MTDPKAIQPS ELDQLPDRDP EETAEWQASL DAVTKAAGPH RAAYLMRRTL ERAEGAGLAL
PKLLETDYVN SIPTADEPAV DGDEDLEQRI TAWNRWNAAA MVTRGSKHGV GGHIATFASA
AWLYETGFNH FFKGKEGDGS GDQLYVQGHA SPGIYARAFL DGRLTEDHLD NFRRESGGNG
LPSYPHPRRL PWLWEFPTVS MGLGPISAIY QARFNRYLTN RGIKDLTNSH VWAFLGDGEM
DEPESTTALT LASREGLDNL TFVINCNLQR LDGPVRANFK IVQELEAQFR GAGWNVVKSL
WGTAWDELFQ LDTNGALVRR LREVPDAQVQ TYQTRDAAYI REDFFGKDPE LAAMAKLLSD
DKILECFHYS RGGHEARKVY AAYKAALAHK GAPTVILAQT VKGHTLGTGF ASKNANHQMK
KLSVDEFKDM RDLLGLPIKD SDFTDGVVPY GHPGADSPEV RYLQERRAAL GGPAPARRVH
PVAPLPAPAE KAFASFDKGS GSQSVATTMA FVRLVKDLVR DKETGKRWVP IVPDEARTFG
MESLFPSLGI YSPKGQTYEP VDRDQLMYYK EAENGQILNE GITEAGSMAD FIAASTSYAT
HGETMIPFYI FYSMFGWQRT ADQMWQLGDQ LGRGFLVGAT AGRTTLTGEG LQHADGHSPA
IAATNPAALT YDPAFAYEVA AIVKDGLRRM YGEAAPGEDP DVFYYLTVYN EPMPQPAKPS
AAGVDEGIVK GLYRFNTAET AGLTPAANAP RIQLLGSGTA IHWALKAQRL LSEEWGVAAD
VWSATSWTEL RRDAMDADAA LLRGEERVPY LRRALQGAEG PVLAVSDYMR QVPDQIAQWV
EQDYSSLGAD GFGLSDTRDA ARRHFGVDAE SIVVAALAQL ARRGEVKAAA VKEARERYGL
//
