ID A0A1G5E1X6_9ACTN Unreviewed; 889 AA.
AC A0A1G5E1X6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN02745898_1011231 {ECO:0000313|EMBL:SCY20865.1};
OS Streptomyces sp. 136MFCol5.1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1172182 {ECO:0000313|EMBL:SCY20865.1, ECO:0000313|Proteomes:UP000199326};
RN [1] {ECO:0000313|EMBL:SCY20865.1, ECO:0000313|Proteomes:UP000199326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=136MFCol5.1 {ECO:0000313|EMBL:SCY20865.1,
RC ECO:0000313|Proteomes:UP000199326};
RA de Groot N.N.;
RL Submitted (OCT-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; FMVI01000001; SCY20865.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5E1X6; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000199326; 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:SCY20865.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199326};
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 484..710
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT REGION 1..21
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 889 AA; 97727 MW; 6593BE06EEB53DF6 CRC64;
MTDPVGKLPS ELDQLPDRDP EETAEWAASL DAVTKAAGPH RAAYLMRRSL QHAEGAGLAL
PKLLETDYVN SIPTAAEPAF DGDLEMESRI TAWNRWNAAA MVTRGARHGV GGHIATFASA
AWLYETGFNH FFRGKEGDGS GDQLYIQGHA SPGIYARAFL DGRLSEQQLD NFRQEAGGDG
LPSYPHPRRL PWLWEFPTVS MGLGPLSAIY QARFNRYLAN RNIKDTSNSH VWAFLGDGEM
DEPESTAALA LAAREKLDNL TFVINCNLQR LDGPVRANFR VVQELEGAFR GAGWNVIKTL
WGSAWDELFQ LDTTGALVRR LRQVPDAQFQ TYATRDVAYI REHFFGAEPA LAELAKLLTD
AKIAECFYTS RGGHEARKVY AAYRAAVEHK GAPTVILAQT VKGYTLGKGF ESKNANHQMK
KLSIDEFKGM RELLGLPIPD SAFDDGPVPY GHPGADSPEV RYLQERRAAL GGPAPARRVH
AVALPQPEER AFAALKKGSG KQEMATTMAF VRLVKDLMRD KETGRRWVPI VPDEARTFGM
ESLFPSAGIY SPLGQTYDPV DRDQLMYYKE AKDGQILNEG ITEAGAMADF IAASTSYATH
GETMIPFYIF YSMFGWQRTG DQMWQLADQL GKGFIVGATA GRTTLTGEGL QHADGHSHLI
AATNPASLNY DPAFAYEIAV IVKDGLRRMY GPEAENVFYY LTVYNEPKQQ PAMPEGVEDG
IVKGLYRFKE GTPASAEAPR LQLLASGTAI HWALEAQDLL AADWGVTADV WSATSWGELR
REALECDEAL LRGEQRVPYV TQALSGAPGP VLAVSDWMRQ VPDQISQWVE QDWSSLGTDG
FGLSDTRDAA RRHFGVDAPS IAVAALAQLA RRGEVPASAV KEAREKYGL
//
