ID A0A0E3Z211_9GAMM Unreviewed; 897 AA.
AC A0A0E3Z211;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
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:AKC86997.1};
GN ORFNames=WQ53_09805 {ECO:0000313|EMBL:AKC86997.1};
OS Pseudoxanthomonas suwonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=314722 {ECO:0000313|EMBL:AKC86997.1, ECO:0000313|Proteomes:UP000033067};
RN [1] {ECO:0000313|EMBL:AKC86997.1, ECO:0000313|Proteomes:UP000033067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J1 {ECO:0000313|EMBL:AKC86997.1,
RC ECO:0000313|Proteomes:UP000033067};
RX PubMed=26067962;
RA Hou L., Jiang J., Xu Z., Zhou Y., Leung F.C.;
RT "Complete Genome Sequence of Pseudoxanthomonas suwonensis Strain J1, a
RT Cellulose-Degrading Bacterium Isolated from Leaf- and Wood-Enriched Soil.";
RL Genome Announc. 3:e00614-15(2015).
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};
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DR EMBL; CP011144; AKC86997.1; -; Genomic_DNA.
DR RefSeq; WP_052631984.1; NZ_CP011144.1.
DR AlphaFoldDB; A0A0E3Z211; -.
DR KEGG; psuw:WQ53_09805; -.
DR PATRIC; fig|314722.6.peg.2107; -.
DR eggNOG; COG2609; Bacteria.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000033067; Chromosome.
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:AKC86997.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000033067};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 87..294
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 493..705
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 265
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 897 AA; 100323 MW; 9DB7E8EEB9FC4A7E CRC64;
MNWLNEVLQN DPDPVETQEW IESLKAVIDR DGPERAHLLL EDMVELTRRS GAFLPFSPTT
EYVNTIAPTL EAKSPGNADL EWRIRSIIRW NAMATVVRAN RKPGDLGGHI ASFASAATLY
DVGFNHFWRA PSDNHPGDLL FIQGHSAPGI YARSYLEGRI SENQLDNFRM EVDGRGISSY
PHPWLMPDYW QTPTVSMGLG PLAAIYQAQF MKYLEHRGLI AESDRKVWCF IGDGESDEPE
TLGAIALAGR EGLDNLIFVV NCNLQRLDGP VRGNGKIIQE LEGVFRGGGW NVIKLLWGGY
WDALLARDTN GILKKLMMET VDGEYQNCKA FGGAYTRENF FGKYPETAAM VAGLSDDDIW
RLNRGGHDPH KVYAAYHQAV NTKGMPTVIL AKTVKGYGMG SSGESLNPTH QTKKLDDDAV
RAFRDRFNIP LTDKQLEEAE QVPFYHPGED SPEVQYLKER RAALGGYLPQ RRQKASKSFT
VPALDKFERL LKDSGERTYS TTMAFVQTLN IALRDKELGP HLVPIVADEA RTFGMEGLFR
QIGIYAPFGQ KYKPVDSDQL MYYREDQAGQ VLQQGISEPG AIASWMAAGT SYSVSNVPML
PFYIYYSMFG FQRVGDIAWQ AADMRTRGFL LGGTAGRTTL NGEGLQHEDG HSQVQAGFIP
NVRSYDPTFG YEVTVLLQHG MKAMMEDQID EYWYLTLMNE NYAHPEMPAG AEQGIIKGMY
LLKDAGKPKK GELRVQLLGS GTILREAIAA AEVLDKDFGV TADIWSCPSF NELRRDGFDV
ERWNRMNPEA KTPRKAYVTE LLEGRQGPAI AATDYVRGFA DQIRAFVPMQ YTVLGTDGFG
RSDTRANLRR FFEVDRYYIA HAAIAALAKE GKMTGKDVAR AIKQYKIDPE KANPVGV
//
