ID A0A099CTK1_9GAMM Unreviewed; 898 AA.
AC A0A099CTK1;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
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:KGI76947.1};
GN ORFNames=HNQ86_002524 {ECO:0000313|EMBL:MBB6185179.1}, LF63_0113635
GN {ECO:0000313|EMBL:KGI76947.1};
OS Oleiagrimonas soli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Oleiagrimonas.
OX NCBI_TaxID=1543381 {ECO:0000313|EMBL:KGI76947.1, ECO:0000313|Proteomes:UP000029708};
RN [1] {ECO:0000313|EMBL:KGI76947.1, ECO:0000313|Proteomes:UP000029708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3.5X {ECO:0000313|EMBL:KGI76947.1,
RC ECO:0000313|Proteomes:UP000029708};
RA Fang T., Wang H.;
RT "Xanthomonadaceae 3.5X direct submission.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB6185179.1, ECO:0000313|Proteomes:UP000560000}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 107085 {ECO:0000313|EMBL:MBB6185179.1,
RC ECO:0000313|Proteomes:UP000560000};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) 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:KGI76947.1}.
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DR EMBL; JROI01000015; KGI76947.1; -; Genomic_DNA.
DR EMBL; JACHET010000001; MBB6185179.1; -; Genomic_DNA.
DR RefSeq; WP_043102665.1; NZ_KN196470.1.
DR AlphaFoldDB; A0A099CTK1; -.
DR STRING; 1543381.LF63_0113635; -.
DR HOGENOM; CLU_009154_2_0_6; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000029708; Unassembled WGS sequence.
DR Proteomes; UP000560000; 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:KGI76947.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029708};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 139..296
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 486..704
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 235
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"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 898 AA; 101144 MW; 8FE5048530A5F8EF CRC64;
MDQMQDILDQ DLDPTETREW IDSLNAVITA DGPQRAHFLL DRMVDATRRA GGYLPFDPTT
EYVNTIPPHM EAKSPGDAAL EWRIRSLIRW NAMAMVVRAN RKPGSLGGHI ASFASSATLY
DVGFNHFWRA PSEDHPGDLV FYQGHSSPGI YARSFMEGRF SAEQMDLFRM EVVGKGQGLS
SYPHPWLMPD YWQVPTVSMG LGPIQAIYQA QFWKYLEHRG LMPKTDRKIW CFMGDGECDE
PESLGAISLA GREKLDNLVF VINCNLQRLD GPVRGNGKII QELEGVFRGA GWNVLKLVWG
SYWDPLLARD DKGVLRKLMM ETLDGEYQAC KAFGGAYTRE HFFNKYPETK AMVANLSDDD
IWRLNRGGHD PHKVYAAYHA ASHTGGMPTV ILAKTVKGYG MGEAGESQNP THQQKKLDLD
AVRHFRDRFN IPVPDDKLEE VPYYHPGKDS EEVQYMLERR KALGGALPQR RGASSKTFKA
PDLEFYKQIT KGSGDREIST TMSLVRGMNL LLRDKEIGQR VVPIVSDEAR TFGMEGMFRQ
IGIYAPFGQK YRPQDADQLL YYREDTKGQV LQEGISEAGG MSAWMAAATS YSISDQPMLP
FFIYYSMFGF QRIGDLAWAA GDMRSRGFLI GGTAGRTTLN GEGLQHEDGH SHLLAGTIPN
CKAYDPTFSY EVAIILQDGV RRMLAEQEDV YYYLTVMNEN YAHPDMPEGC EDGVLKGMYL
LQDVGKTKKN TPRVQLLGSG TILREAIAAA ELLKNDFGVE ADIWSCTSFV ELRRDGFDAE
RWNRLHPEAK QSREAYVTQC LKDREGPVVA ATDYVREFAD QIRAFMPDGK RYTVLGTDGY
GRSDTREHLR SFFEVDRYWI AHAALAALAR DGAVNAKDVT RAIKQYKLDV DKPNPLSV
//
