ID A0A0Q6X5L3_9BURK Unreviewed; 901 AA.
AC A0A0Q6X5L3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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 Name=aceE {ECO:0000313|EMBL:KQV96810.1};
GN ORFNames=ASC87_24765 {ECO:0000313|EMBL:KQV96810.1};
OS Rhizobacter sp. Root1221.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736433 {ECO:0000313|EMBL:KQV96810.1, ECO:0000313|Proteomes:UP000051465};
RN [1] {ECO:0000313|EMBL:KQV96810.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQV96810.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV96810.1, ECO:0000313|Proteomes:UP000051465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1221 {ECO:0000313|EMBL:KQV96810.1,
RC ECO:0000313|Proteomes:UP000051465};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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|ARBA:ARBA00003157, 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:KQV96810.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMDI01000022; KQV96810.1; -; Genomic_DNA.
DR RefSeq; WP_056664069.1; NZ_LMDI01000022.1.
DR AlphaFoldDB; A0A0Q6X5L3; -.
DR STRING; 1736433.ASC87_24765; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000051465; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR001849; PH_domain.
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.
DR PROSITE; PS50003; PH_DOMAIN; 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:KQV96810.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051465};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 1..33
FT /note="PH"
FT /evidence="ECO:0000259|PROSITE:PS50003"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 271
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 901 AA; 100945 MW; 6E03D8E9801D4E4B CRC64;
MSALPESFLG ASANDADSQE TREWLDALSA LIETEGGDRA HFLLEQLIDH ARQVGIDMPF
SANTAYVNTI PADKEERCPG NLEMEERLRA YMRWNAMAMV VRANRLHPAD GGDLGGHISS
FASLATMFGA GFNHFWHGAT EDHGGDLLYI QGHSSPGIYA RAFMEGRITE EQLNNFRQEV
DGKGISSYPH PKLMPEFWQF PTVSMGLGPL MAIYQARFLK YLHARGIADT SKRKVWVFCG
DGEMDEPESL GAIGLAAREK LDNLIFVVNC NLQRLDGPVR GNGKIIQELE GEFRGAGWNV
IKLLWGSYWD PLLARDKDEL LRKVMMDTLD GDYQAFKAND GAFVRKNFFG RHPKLLEMVS
KMSDDDIWRL NRGGHDPQKV YAAYHRAVNH KGQPTVLLIK TVKGFGMGKI GEGKNTAHQT
KKMVDEDVKT FRDRFNIPIP DDKIAEVPFY KPADDTPEMR YLHERRKALG GYLPQRRPKA
EEQFTIPPLD TFKATLEATA EGREISTTQA YVRFLTQLLR DKEIGPRTVP ILVDEARTFG
MEGLFRQIGI YNPQGQLYTP VDKDQVMYYR EDKAGQILQE GINEAGGMSS WIAAATSYAT
NNRIMIPFYV YYSMFGFQRI GDLAWAAGDM QARGFLLGGT SGRTTLNGEG LQHEDGHSHI
LAGTIPNCIS YDPTFAHEVG VILHHGLKRM VEKQENVFFY LTLLNENYAM PGLTAGTEEQ
IIKGMYLLQA GAKKTPRVNL LGSGTILRES IAAKELLEKE WGVAANVWSC PSFNELARDG
QDAERWNLLH PTDKPRVPFV AQQLEPHAGP VIASTDYMKS YADQIRAFLP KGRTFKVLGT
DGFGRSDFRS KLREHFEINR HYIVVASLKA LAEEGTVPAA KVAEAIAKYN IKADKINPLY
A
//
