ID A0A1H3P422_9PSEU Unreviewed; 921 AA.
AC A0A1H3P422;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN05216215_104077 {ECO:0000313|EMBL:SDY95904.1};
OS Saccharopolyspora shandongensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=418495 {ECO:0000313|EMBL:SDY95904.1, ECO:0000313|Proteomes:UP000199529};
RN [1] {ECO:0000313|EMBL:SDY95904.1, ECO:0000313|Proteomes:UP000199529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3530 {ECO:0000313|EMBL:SDY95904.1,
RC ECO:0000313|Proteomes:UP000199529};
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; FNOK01000040; SDY95904.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3P422; -.
DR STRING; 418495.SAMN05216215_104077; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000199529; 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:SDY95904.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 160..325
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 503..725
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 254
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 284
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 921 AA; 102531 MW; 416E8166A9ED3E1E CRC64;
MSPLNNDAPV PAQRVRVIRD GLASHLPDID PQETEEWLQS FDSVLSANGQ QRARYLMLRL
LQRARESGVG VPSLTSTDYV NTIPTEQEPW FPGDEETERR YRAWMRWNAA MMVHRAQRPG
IGVGGHISSF ASSASLYEVG FNWFFRGKDH PGGGDHLYIQ GHASPGIYAR AFLEGRLSAD
RLDGFRQEYS HAGPGGGLPS YPHPRLMPDF WEFPTVSMGL GPMNAIYQAR FDRYLHDRGI
KDTSQQRVWA FLGDGEMNEP ESRGLLQVAA NDGLDNLTFV INCNLQQLDG PVRGNGKIIQ
ELEAFFRGAG WNVIKVVWGR EWDSLLHADR DGALVNLMNT TPDGDYQTYK ANDGAFVREH
FFGRDPRTKE MVKHLTDDQI WGLRRGGHDY RKVYAAYKAA TEHHGQPTVI LAKTIKGYGL
GPHFEGRNAT HQMKKLTLDD LKLFRDSLRI PISDDELDPY LPPYYHPGQD APEIQYLQDR
RRQLGGYLPE RRAKTKPLVL PGDKVYEVVR RGSGKQEVAT TMAFVRLLKD LAKDREIGAR
IVPIIPDEAR TFGMDSMFPS QKIYNPLGQL YTPVDYQLML AYRESEQGQI LHEGINEAGS
TSSFTAAGTS YATHGEPMIP VYIFYSMFGF QRTGDSFWAA ADQMARGFVL GATAGRTTLT
GEGLQHADGH SQLIAATNPA VVAYDPAWSF EVAHIVKDGL RRMFGENPED VFYYLTIYNE
PYQQPAEPAD LDVDGLLRGL YRYQAAPGGS GPRAQILSSG VIMPLALKAQ QMLAEEWGVQ
ADVWSATSWS QLRREAEAAD RHNLMHPEAE PQVPHVTRAL ADAAGPVVAV SDWMRAVPDL
IRPWVPGDMV SLGADGFGFS DTRPAARRVF LVDAESTVVA TLAALARTGQ VDKAKVIEAT
RRYRLDDVQA AGPQTSDPGV A
//
