ID D4XBU0_9BURK Unreviewed; 902 AA.
AC D4XBU0;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
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:EFF75876.1};
GN ORFNames=HMPREF0004_2937 {ECO:0000313|EMBL:EFF75876.1};
OS Achromobacter piechaudii ATCC 43553.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Achromobacter.
OX NCBI_TaxID=742159 {ECO:0000313|EMBL:EFF75876.1, ECO:0000313|Proteomes:UP000004510};
RN [1] {ECO:0000313|Proteomes:UP000004510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43553 {ECO:0000313|Proteomes:UP000004510};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R., Gibbs R.;
RT "Complete sequence of Mobiluncus curtisii ATCC 43063.";
RL Submitted (MAR-2010) 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:EFF75876.1}.
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DR EMBL; ADMS01000062; EFF75876.1; -; Genomic_DNA.
DR RefSeq; WP_006219005.1; NZ_GG770409.1.
DR AlphaFoldDB; D4XBU0; -.
DR PATRIC; fig|742159.3.peg.3872; -.
DR eggNOG; COG2609; Bacteria.
DR HOGENOM; CLU_009154_2_0_4; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000004510; 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:EFF75876.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 147..302
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 498..711
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
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 902 AA; 100860 MW; 062B737B14D61D42 CRC64;
MSSFAQAGAP QAANDEDTLE TQEWLEALAA VLDREGPQRA HYLLERLIDE ARRSGAHIPF
SPNTAYVNTI PPGLEPAHPG NLELETRIRS YVRWNAMAMV VKANKHNPPD GGDLGGHIAS
FASLATMIGC GQNHFWHAED ENHGGDLVYF QGHTSPGMYG RAYLEGRLTE DQLNHFRQEV
DGKGLSSYPH PKLMPDFWQF PTVSMGLGPL MAIYQARFLK YLHARGIADT SKRKVWVFCG
DGEMDEPESL GAIALAAREK LDNLIFVVNC NLQRLDGPVR GNGKIIQELE GDFRGSGWNV
IKLIWGGYWD PLLAHDKEGI LRQIMEDTVD GEYQAYKAND GKFVREHFFG KHPKLLEAVS
RMSDEDIWRL NRGGHDPHKV YAAFDAATSH TGQPTVILAK TIKGYGMGHV GQAKNPTHQQ
KKLELESIRE FRDRFGIPIP DDQLESLPYF KPAEDSPEMK YLHERRAALG GYLPRRRAKA
DEKLKAPALD AFKAVLEPTA EGREISTTQA FVRILNQVLR DKDLGPRVVP ILADESRTFG
MEGLFRQIGI YAPEGQKYTP VDKDQVMYYK ESADGQLLQE GINEAGAMSS WIAAATSYSS
NNRIMIPFFI YYSMFGFQRI GDLAWAAGDM QARGFLLGGT AGRTTLNGEG LQHEDGHSHI
LASTIPNCVS YDPTFGHELA VIIQHGLKRM VEDQENVYYY LTVMNENYPQ PGLTQGDEEG
IIKGMYKLKS HGKGKNRVQL MGSGTILREV MAAQELLEAD WGVASDLWSV TSFTELRRNG
LDVERHNMLH PDEKKPQVAY VTEQLAKTEG PIIASTDYMK LFADQIRPFV PKGREYKVLG
TDGFGRSDFR SKLREHFEVD RHFVVVAALR ALADEGKVPV AKVAEAIKKY GINPNKANPQ
YA
//
