ID A8TWM8_9PROT Unreviewed; 793 AA.
AC A8TWM8;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00017172, ECO:0000256|PIRNR:PIRNR000156};
DE EC=1.2.4.1 {ECO:0000256|PIRNR:PIRNR000156};
GN ORFNames=BAL199_30167 {ECO:0000313|EMBL:EDP63129.1};
OS alpha proteobacterium BAL199.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=331869 {ECO:0000313|EMBL:EDP63129.1, ECO:0000313|Proteomes:UP000003417};
RN [1] {ECO:0000313|EMBL:EDP63129.1, ECO:0000313|Proteomes:UP000003417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL199 {ECO:0000313|EMBL:EDP63129.1,
RC ECO:0000313|Proteomes:UP000003417};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (OCT-2007) 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|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR000156-1};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|PIRNR:PIRNR000156};
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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:EDP63129.1}.
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DR EMBL; ABHC01000016; EDP63129.1; -; Genomic_DNA.
DR AlphaFoldDB; A8TWM8; -.
DR STRING; 331869.BAL199_30167; -.
DR eggNOG; COG2609; Bacteria.
DR Proteomes; UP000003417; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
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 InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF4; 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 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 Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000156-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000156-1};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000156};
KW Pyruvate {ECO:0000256|PIRNR:PIRNR000156};
KW Reference proteome {ECO:0000313|Proteomes:UP000003417};
KW Thiamine pyrophosphate {ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 424..629
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT BINDING 171
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"
FT BINDING 203
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 793 AA; 86504 MW; 2B0F0B7B28EB6647 CRC64;
MTGKPAEPID PLKIDLMRAL ERKVLWHAMW TIHNANHIRE SRDHIKVGGH QASCASVATL
MTALYFDVLR PQDRVAVKPH ASPIFHAIQY MMGRQSRDAL ERFRAYGGAQ SYPSRTKDAD
EVDFSTGSVG LGVAMTLFAS MVQDYVQLHN LVQDPEITAQ GPGRMISVLG DAELDEGNIY
EAMLEGWKYD VRNLWWIIDY NRQSLDGVVS DGLFRKIQEF FKTVDWQVVT LKYGKKLERV
FKLPGGDVLE KWIDDCPNEI YSALTFKGQS GEPGAWRERL KLDLKGVSGI KAILDDHDDE
ALHTLMTNLA GQDMEAVLEA FHAVEDDAPR CFIAYTIKGY GTPLAGHKDN HAGLMTPDQM
TRFKAQNGIA DGQEWDLFAE AGLPAQTLKD YVKGVSFNAP GSRIHSAPKV ELPDRLNLRI
NKTMATQQAF GSILNELARG NSALASRIVT TSPDVTVSTN LGPWVNQRGI FSLDVRNDVF
RDEQVASAQK WMRHGGGQHL ELGIAESNLF ILLGALGLSG PLFGTRLLPV GTLYDPFIQR
GLDSLNYACY QGARFMVVAT PAGITLAPEG GAHQSISTPL IGLGQPGLSS FEPAYVDELA
AIMRWGFEHM QADDGGSVYL RLSTRAVDQP DRTLGDAQTA DLLAGAYWQI EPKAGAELAL
LYSGPVVPEV LQAYEELAED VPGLGVLAVT SNDRLYHDWQ GGLRRRNGSG AGGSLVERLL
SPLAPNAGLV TVHDGHPAAL SWIGSATGRR LYPLGVSSFG QSGDIPDLYA HYGLDADAIV
NMAATACLEA ARA
//
