ID A0A1P8XTT6_9ACTN Unreviewed; 909 AA.
AC A0A1P8XTT6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=BV401_15215 {ECO:0000313|EMBL:AQA11622.1};
OS Streptomyces autolyticus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=75293 {ECO:0000313|EMBL:AQA11622.1, ECO:0000313|Proteomes:UP000187851};
RN [1] {ECO:0000313|Proteomes:UP000187851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC0516 {ECO:0000313|Proteomes:UP000187851};
RA Yin M., Jiang M., Lu T.;
RT "Streptomyces autolyticus CGMCC0516 complete genome sequence.";
RL Submitted (JAN-2017) 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; CP019458; AQA11622.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P8XTT6; -.
DR STRING; 75293.BV401_15215; -.
DR KEGG; sauo:BV401_15215; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000187851; 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:AQA11622.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 149..306
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 493..715
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 909 AA; 101317 MW; BC54B38CA44F3BF3 CRC64;
MASGSDRNPI IIGGLPSQVP DFDPEETQEW LDSLDAAVDE RGRERARYLM LRLIERAREK
RVAVPEMRST DYVNTIATKD EPFFPGNEEI ERKVLNATRW NAAVMVSRAQ RPGIGVGGHI
ATFASSASLY DVGFNHFFRG KDHDSGDQIF FQGHASPGIY ARAFLLDRLS EAHLDGFRQE
KSKLGHALSS YPHPRSMPDF WEFPTVSMGL GPLGAIFQAR MNRYMEARGV ADTSNSHVWA
FLGDGEMDEP ESLGQLSLAA REGLDNLTFV VNCNLQRLDG PVRGNGKIIQ ELESQFRGAG
WNVIKLVWDR TWDPLLARDR DGILVNKLNT TPDGQFQTYA TETGAYIREH FFGEDQRLRK
MVEGMTDDQV LHLGRGGHDH KKIYAAYSAA KAHKGQPTVI LAQTVKGWTL GPNFEGRNAT
HQMKKLTVDD LKRFRDRLHL PIPDKELESG LPPYYHPGRD SEEIQYMHDR RKALGGYAPT
RVVRTKPLQL PGDKTYATLK KGTGQQQIAT TMAFVRLLKD LMRDKEIGKR FVPIAPDEYR
TFGMDSLFPS AKIYSPLGQT YESVDRELLL AYKESATGQM LHDGISEAGC TASLIAAGSA
YATHGEPLIP VYVFYSMFGF QRTGDQFWQM ADQLARGFVL GATAGRTTLT GEGLQHADGH
SQLLASTNPA VVAYDPAFGF EIAHIVQDGL RRMYGENSED VFYYLTVYNE PIQHPAEPEN
VDREGILKGL YRYRQGEKGA IPANILASGV AVPWAVEAQR VLAEDWNVKA DVWSATSWNE
LRRDAVETEE HNLLHPEEEQ RVPYVTRKLA DAEGPKVAVS DWMRAVPDQI ARWVPGTYQS
LGADGFGFAD TRGAARRFFH IDAESIVLGV LTELARDGKI DRSVLKQAID RYQLLDVAAA
DPGPAGGDA
//
