ID A0A2U1C6S2_9BURK Unreviewed; 885 AA.
AC A0A2U1C6S2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ORFNames=C8D04_1790 {ECO:0000313|EMBL:PVY56531.1};
OS Simplicispira sp. 125.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Simplicispira.
OX NCBI_TaxID=2135643 {ECO:0000313|EMBL:PVY56531.1, ECO:0000313|Proteomes:UP000245599};
RN [1] {ECO:0000313|EMBL:PVY56531.1, ECO:0000313|Proteomes:UP000245599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=125 {ECO:0000313|EMBL:PVY56531.1,
RC ECO:0000313|Proteomes:UP000245599};
RA Chistoserdova L.;
RT "Synthetic bacterial communities of pure cultures isolated from sediment of
RT Lake Washington, USA.";
RL Submitted (APR-2018) 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:PVY56531.1}.
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DR EMBL; QEKM01000001; PVY56531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U1C6S2; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000245599; 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:0016744; F:transketolase or transaldolase activity; IEA:UniProt.
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; IPR017600; Alpha-ketoglut_DH.
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; IPR033248; Transketolase_C.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00759; aceE; 1.
DR NCBIfam; TIGR03186; AKGDH_not_PDH; 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; PF02780; Transketolase_C; 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:PVY56531.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000245599};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 114..316
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 503..716
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT DOMAIN 749..790
FT /note="Transketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02780"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 278
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 885 AA; 96356 MW; B18FCA5AFC6C8B4C CRC64;
MNALTPHAIL QVPQSQDIDP EETAEWRDAF LALVATQGPE RARHLLQEIV GVARAQRVGW
QPDLNTPYVN TVAVQEQGVF PGDLAIEERL GSIIRWNALA MVVRANQAYG ELGGHIASYA
SAADLFESGF NHFFHAREGL GEGQHRGDLV FFQPHSAPGV YARAFLEGRL SEQDLMHYRQ
ELTAPTVGAQ GLSSYPHPWL MPDFWQFPTG SMGIGPISSI YHARFMRYLT HRNLLDCTGR
KVWGVFGDGE MDEPESTSAL TLASREGLDN LVWVVNCNLQ RLDGPVRGNG RIIDELERLF
AGAGWNVVKL VWGSDWDGLF ARDLTGALVR TLEATVDGQM QTFAAKDGRF NRDNFFGQSP
ELAALAQGMT DEQIDRLKRG GHDLVKIHAA YAAAAAHRGQ PTVILAHTKK GYGMGTAGQG
KMTTHSQKKL DGADLIEFRN RFNLPLTDEQ ATSLAFYKPF EDSPEMRYLR SHRQQLGGYL
PHREAICEPL PVPPIASYAQ FALQAAGKEM STTMAFVRML GTLMKDPALG PRIVPIVADE
ARTFGMANLF KQVGIYSSVG QRYAPEDIGS VLAYREALDG QILEEGISEA GAIASWTAAA
TSYSVHGLAM LPFYIYYSMF GFQRVGDAIW AAADQRARGF LLGATSGRTT LGGEGLQHQD
GTSHLVAATI PNCKAYDPAY AGEMAVIVDA GMREMVTEQR DVFYYVTLMN ENYAQPDLPE
GAAEGVLRGC YVFNSFQRLP DGRERSISSK NVTLLGSGAI LTEVVKAAEL LAAEGIEATV
LSVTSWSELA RDGQACEQRA LAGEAAPGEP WLTQQLAATH GPVIAATDYV RAVPDSVRAL
VPAGRRYLTL GTDGFGRSDT RAALRAFFGV DALAIAKAAK FALEG
//
