ID A0A0N0K7W9_9PROT Unreviewed; 785 AA.
AC A0A0N0K7W9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|PIRNR:PIRNR000156};
DE EC=1.2.4.1 {ECO:0000256|PIRNR:PIRNR000156};
GN ORFNames=IP70_16945 {ECO:0000313|EMBL:KPF83898.1};
OS alpha proteobacterium AAP38.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1523418 {ECO:0000313|EMBL:KPF83898.1, ECO:0000313|Proteomes:UP000037884};
RN [1] {ECO:0000313|EMBL:KPF83898.1, ECO:0000313|Proteomes:UP000037884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP38 {ECO:0000313|EMBL:KPF83898.1,
RC ECO:0000313|Proteomes:UP000037884};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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|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|PIRNR:PIRNR000156};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC 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 -!- PATHWAY: Metabolic intermediate biosynthesis; 1-deoxy-D-xylulose 5-
CC phosphate biosynthesis; 1-deoxy-D-xylulose 5-phosphate from D-
CC glyceraldehyde 3-phosphate and pyruvate: step 1/1.
CC {ECO:0000256|ARBA:ARBA00004980}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family. DXPS subfamily.
CC {ECO:0000256|ARBA:ARBA00011081}.
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:KPF83898.1}.
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DR EMBL; LJHR01000026; KPF83898.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0K7W9; -.
DR STRING; 1523418.IP70_16945; -.
DR PATRIC; fig|1523418.3.peg.1563; -.
DR OrthoDB; 9773339at2; -.
DR Proteomes; UP000037884; Unassembled WGS sequence.
DR GO; GO:0008661; F:1-deoxy-D-xylulose-5-phosphate synthase activity; IEA:UniProtKB-EC.
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:0016114; P:terpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR005477; Dxylulose-5-P_synthase.
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; IPR005475; Transketolase-like_Pyr-bd.
DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF4; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR Pfam; PF13292; DXP_synthase_N; 1.
DR Pfam; PF17831; PDH_E1_M; 1.
DR PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Isoprene biosynthesis {ECO:0000256|ARBA:ARBA00023229};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000156-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000156-1};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000156};
KW Pyruvate {ECO:0000256|PIRNR:PIRNR000156};
KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977};
KW Thiamine pyrophosphate {ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 423..628
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 199
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 201
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 785 AA; 85964 MW; B750564B69FAC97C CRC64;
MPDIRPAIPG AARDDRHLAH LRALEKKALW LSTWMIHNAN HLRPSRDGLK VGGHQASSAS
MVSLMTALFF DVLRPQDRVA VKPHASPVFH AIQYLMGRQT REKMERFRAF GGAQSYPSRT
KDTDDVDFST GSVGLGVAVT AFASMVQDYV RLKGLSDQPE GRMVALVGDA EMDEGNVFEA
MLEGWKHDLR NAWWIIDYNR QSLDSVVSDK LWEPITGMFR SLDWNVVIMK YGRLLEAAFL
EPGGEALRHW IDTCPNQLYA ALCFKGGAAW REALIRDLGT TSGIRGLLDS HDDAMLARLM
TNLAGHDLPT ILDTFHAAAN GPDAERPACF VAYTVKGMGL PFQGHKDNHS GLMNLEQMAA
FKAQCGIKDG QEWEPFAGLD VDVEDLKRFL TEEVPFTATP TRRLSAGFVP VPERLDVSVT
ERMSTQEGFG KVLAELAKGD TELASRIVTT SPDVTVSTNL GAWVNRRGLF DRHERHDIFK
EQKVVSAQRW QGDPQGQHIE LGIAEHNLFL MLAALGLSHD LFGARLLPVG TLYDPFVMRG
LDAFNYALYQ DSRFMLVATP SGVTLAPEGG AHQSIATPLI GMGLPKLSSF EPAYVDELAV
IMRWGFAHMQ KPDGGSLYLR LSTRSLEQPS RPLDAEAVID GGYWLRPPAP DADLTLIYMG
ALAPEVLSAH AQLLEDVPGA GLLAVTSADR LHQGWMAARR ARQAGQVAVA PVERLLSTLP
ATARLVTITD GHPSALSWLG GVRGHKVAAL GVETFGQSAD LPDLYAALRL DADAIIDAVA
RVLLE
//
