ID A0A2A3H6X4_9ACTN Unreviewed; 910 AA.
AC A0A2A3H6X4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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=BKI49_10805 {ECO:0000313|EMBL:PBC64165.1};
OS Streptomyces sp. Tue6028.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2036037 {ECO:0000313|EMBL:PBC64165.1, ECO:0000313|Proteomes:UP000217789};
RN [1] {ECO:0000313|EMBL:PBC64165.1, ECO:0000313|Proteomes:UP000217789}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tue6028 {ECO:0000313|EMBL:PBC64165.1,
RC ECO:0000313|Proteomes:UP000217789};
RA Greule A., Flemming S., Bechthold A.;
RT "The Draft Genome Sequence of Streptomyces sp. Tue6028 - Producer of
RT Polyketomycin and Foxicin.";
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};
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:PBC64165.1}.
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DR EMBL; MLCE01000012; PBC64165.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3H6X4; -.
DR Proteomes; UP000217789; 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:PBC64165.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217789};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 150..307
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 493..716
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 277
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 910 AA; 101329 MW; FB825DCF8C373C82 CRC64;
MASGSDRNPI IIGGLPSQVP DFDPEETQEW LDSLDAAVDQ RGRERARYLM LRLIERAREK
RVAVPEMRST DYVNTIATKD EPFFPGNEEI ERKVLNATRW NAAVMVSRAQ RPGIGVGGHI
ATFASSASLY DVGFNHFFRG KDEGDGGDQV FFQGHASPGI YARAYLLDRL TEEQLDGFRQ
EKSKYPNGLS SYPHPRSMPD FWEFPTVSMG LGPLGAIFQA RMNRYMEARE IADTSKSHVW
AFLGDGEMDE PESLGQLSIA AREGLDNLTF VVNCNLQRLD GPVRGNGKII QELESQFRGA
GWNVIKLVWD RTWDPLLAQD RDGILVNKLN ITPDGQFQTY ATETGAYIRQ HFFGDDHRLR
AMVEHMTDDQ VLHLGRGGHD HKKIFAAFSA AKAHKGQPTV ILAQTVKGWT LGPNFEGRNA
THQMKKLTVA DLKHFRDRLH LPISDKQLED GLPPYYHPGR DSEEIQYMHD RRKGLGGYVP
TRLVRAKPLA LPDDKTYASV KKGSGQQSIA TTMAFVRLLK DLMRDKEIGR RFVLIAPDEY
RTFGMDSFFP SAKIYNPLGQ QYEAVDRDLL LAYKESPTGQ MLHDGISEAG CTASLIAAGS
AYATHGEPLI PVYVFYSMFG FQRTGDQFWQ MADQLARGFV LGATAGRTTL TGEGLQHADG
HSQLLASTNP GCVAYDPAYG YEIAHIVQDG LRRMYGPDAE DVFYYLTVYN EPIQHPAEPE
NVDVEGILKG LHRIGEGTSG SIPAQILASG VAVPWAIEAQ RILAEEWNVK ADVWSATSWN
ELRREAVEVE RHNLLHPEEE QRVPYVTQRL SAVQGPFVAV SDWMRSVPDQ ISRWVPGTYQ
SLGADGFGFA DTRGAARRFF HIDAQSIVVA VLTELAREGK VDRSVLKQAI DRYQLLDVAA
ADPGAAGGDA
//
