ID A0A0Q8BB94_9PSED Unreviewed; 881 AA.
AC A0A0Q8BB94;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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:KQZ94733.1};
GN ORFNames=ASD60_01685 {ECO:0000313|EMBL:KQZ94733.1};
OS Pseudomonas sp. Root562.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1736561 {ECO:0000313|EMBL:KQZ94733.1, ECO:0000313|Proteomes:UP000051426};
RN [1] {ECO:0000313|EMBL:KQZ94733.1, ECO:0000313|Proteomes:UP000051426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root562 {ECO:0000313|EMBL:KQZ94733.1,
RC ECO:0000313|Proteomes:UP000051426};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ94733.1, ECO:0000313|Proteomes:UP000051426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root562 {ECO:0000313|EMBL:KQZ94733.1,
RC ECO:0000313|Proteomes:UP000051426};
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:KQZ94733.1}.
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DR EMBL; LMGK01000001; KQZ94733.1; -; Genomic_DNA.
DR RefSeq; WP_056852320.1; NZ_LMGK01000001.1.
DR AlphaFoldDB; A0A0Q8BB94; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000051426; 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; 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:KQZ94733.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 135..287
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 467..691
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 257
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 881 AA; 99452 MW; 5A08E166FC6669DE CRC64;
MQDLDPVETQ EWLDALESVL DKEGEDRAHY LMTRMGELAT RSGSQLPYAI TTPYRNTIPV
THEARMPGDL FMERRIRSLV RWNAMAMVMR TNLKDSDLGG HISSFASSAT LYDIGFNYFF
QAPTDEHGGD LIYFQGHTSP GVYARAFMEG RITEEQMNNF RQEVDGQGLS SYPHPWLMPD
FWQFPTVSMG LGPIQAIYQA RFMKYLEARG FIPAGKQKVW CFLGDGECDE PESLGAISLA
GREKLDNLIF VINCNLQRLD GPVRGNGKII QELEGVFRGA QWNVTKVIWG RFWDPLLAKD
VDGILQRRMD EVIDGEYQNY KAKDGAFVRE HFFNTPELKA MVEDLSDDEI WKLNRGGHDP
YKVYAAYHEA VNHKEQPTVI LAKTIKGYGT GAGEAKNTAH NTKKVDVESL KLFRDRFDIP
VKDEELENLP FFKPEPNSAE ARYLSERRTA LGGFVPQRRA QSFSVPTPDL DTLKAILDGS
GDREISTTMA FVRILAQLVK DKEIGPRIVP IIPDEARTFG MEGMFRQLGI YSSVGQLYEP
VDKDQVMFYK EDKKGQILEE GINEAGAMSS FIAAGTSYSS HNQPMLPFYI FYSMFGFQRI
GDLAWAAGDS RTRGFLIGGT AGRTTLNGEG LQHEDGHSHL LAATIPNCRT YDPTYGYELA
VIIQDGMKKM TEEQQDVFYY ITVMNESYQQ PAMPAGAEEG IKKGMYLLEE DTREAAHHVQ
LMGSGTILRE VREAAKILRE QFNVGADVWS VTSFNELRRD GLAVERTNRL HPGQKPKLSY
VEECLNGRKG PVIASTDYMK LFAEQIRQWV PSKEFKVLGT DGFGRSDSRK KLRHFFEVDR
HFVVLAALEA LADRGDIEPK VVAEAIAKFG INPEKLNPLD C
//
