ID A0A1G1LQC8_9BACT Unreviewed; 894 AA.
AC A0A1G1LQC8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=A2Z88_03835 {ECO:0000313|EMBL:OGX07378.1};
OS Omnitrophica WOR_2 bacterium GWA2_47_8.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801840 {ECO:0000313|EMBL:OGX07378.1, ECO:0000313|Proteomes:UP000178620};
RN [1] {ECO:0000313|EMBL:OGX07378.1, ECO:0000313|Proteomes:UP000178620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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|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:OGX07378.1}.
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DR EMBL; MHFY01000089; OGX07378.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1LQC8; -.
DR STRING; 1801840.A2Z88_03835; -.
DR Proteomes; UP000178620; 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:OGX07378.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 85..304
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 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 894 AA; 100587 MW; C722C9659F093DDD CRC64;
MTGDDVVKNR SSEVEEIEIK EWLSSLDYVL THGTEEQAKK ILQQLQIRAQ EAGVTLPFVA
NTPYINTIPP EKQPPFPGNR DIERRIKSII RWNAMAMVVG GNKAEAGIGG HISTFASAAT
LFEMGFNHFF RARNDNFCGD FVYFQGHASP GVYARAFVEG RLTEKNLENF RRELQPGGGL
SSYPHPWLMP NFWQFPTVSM GLAPLTGIYQ ARFQRYLEDR GLKPKDDAKV WVFMGDGECD
EPESLGAIHL GSREKLDNLI FVINCNLQRL DGPVRGNGKI IQELEALFRG AQWNVVKVIW
GSDWDPLLEK DSEGLLAKRM GEVVDGQYQK YSVETGAYIR NDFFGHDQKL LDMVKHLSDG
DLQKMRRGGH DPLKVYAAYK TAVEFKGAPT VILAKTIKGY GLGESGEGKN ITHQQKKLNE
DELKEFRTRF GIPVSDEEVV NTPFYRPPED SEEMKYLRAR REALGGYMPS RQETSTPIKT
PAEELFEEFN KGTEGREVST TMAYVRILSK LLKDPEVGKL IVPIIPDEAR TFGMEALFRQ
CGIYSHVGQN YEPVDKDSLI YYKEATDGQI LEEGINEAGA MGSFIAAGTC YSTQGINTMP
FYTYYSMFGP QRVGDLIWAA ADSRCRGFLV GATSGRTTLN GEGLQHQDGH SHLLLSSVPT
CVAYDPAFAY ELAVIIRDGI YRMYEKQENI FYYLSVGNEN YAMPAMPDGV KDGILKGMYR
FQSSDMKTPK LRAHLFGSGA IMNQVIEAQK ILEEKYKVAS DIWSITSYNE LRREALDVER
TNVLNPLEKP KISYITQNLV KEKGVFVAAS DNMKALPDSI GKWFPRPLLS LGTDGFGRSD
SRPALRDFFE VDARHIVYAT LVCLYRDKEI GEDVLKKAAK DLKINPKKLN PMIS
//
