ID A0A1Q5KP58_9ACTN Unreviewed; 915 AA.
AC A0A1Q5KP58;
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=AMK32_17090 {ECO:0000313|EMBL:OKJ83357.1};
OS Streptomyces sp. CB01883.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703943 {ECO:0000313|EMBL:OKJ83357.1, ECO:0000313|Proteomes:UP000186398};
RN [1] {ECO:0000313|EMBL:OKJ83357.1, ECO:0000313|Proteomes:UP000186398}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01883 {ECO:0000313|EMBL:OKJ83357.1,
RC ECO:0000313|Proteomes:UP000186398};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKJ83357.1}.
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DR EMBL; LIWA01000003; OKJ83357.1; -; Genomic_DNA.
DR RefSeq; WP_073893589.1; NZ_LIWA01000003.1.
DR AlphaFoldDB; A0A1Q5KP58; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000186398; 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:OKJ83357.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000186398};
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..721
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 915 AA; 101894 MW; D936CDAAC9A30F92 CRC64;
MASGSDRNPI IIGGLPSQVP DFDPEETQEW LDSLDAAVDE RGRERARYLM LRLIERARER
RVAVPEMRST DYVNTIPTKS EPFFPGNEEI ERRILNATRW NAAVMVSRAQ RPGIGVGGHI
ATFASSASLY DVGFNHFFRG KDEGDGGDQV FFQGHASPGI YARAYLLDRL TDTQLDGFRQ
EKSKYPDGLS SYPHPRSMPD FWEFPTVSMG LGPLGAIYQA RMNRYMQARG IADTSRSHVW
AFLGDGEMDE PESLGQLSLA AREGLDNLTF VVNCNLQRLD GPVRGNGKII QELESVFRGA
GWNVIKLIWD RSWDPLLAQD RDGVLVNRMN TTPDGQFQTY ATESGSYIRD HFFGDDHRLR
AMVENMTDHQ ILMLGRGGHD HRKIYAAYKA ALEHTGQPTV ILAKTVKGWT LGPNFEGRNA
THQMKKLTVD DLKRFRDRLH LPISDKELDS GLPPYFHPGR DSEEIQYMHD RRKQCGGYVP
TRVVRAKPLR LPDDKAYATV KKGTGQQSIA TTMAFVRLLK DLMRDKEIGK RFVLIAPDEY
RTFGMDSFFP SAKIYNPLGQ QYESVDRELL LAYKESPTGQ MLHDGISEAG CTASLIAAGS
AYATHGEPLI PVYVFYSMFG FQRTGDQFWQ MADQLARGFV LGATAGRTTL TGEGLQHADG
HSQLLASTNP ACVAYDPAYA YEIAHIVQDG LRRMYGSSPE HPQGEDVFYY LTVYNEPIQH
PAEPAGVDVE GIVKGVHRIA EATGGSIPAQ VMASGVAVPW ALEAQRILAE DWDVRADVWS
ATSWNELRRE AVACEEHNLL HPEEEQRVPW VTRKLSGSEG PFVAVSDWMR AVPDQIARWV
PGTFQSLGAD GFGFADTRGA ARRFFHIDAQ SIVVAVLTEL AREGKVDRSV LKQAIDRYQL
LDVSAADPGA AGGDA
//
