ID A9BZ36_DELAS Unreviewed; 902 AA.
AC A9BZ36;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 95.
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 OrderedLocusNames=Daci_2498 {ECO:0000313|EMBL:ABX35136.1};
OS Delftia acidovorans (strain DSM 14801 / SPH-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Delftia.
OX NCBI_TaxID=398578 {ECO:0000313|EMBL:ABX35136.1, ECO:0000313|Proteomes:UP000000784};
RN [1] {ECO:0000313|EMBL:ABX35136.1, ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RX PubMed=15240283; DOI=10.1128/AEM.70.7.4053-4063.2004;
RA Schleheck D., Knepper T.P., Fischer K., Cook A.M.;
RT "Mineralization of individual congeners of linear alkylbenzenesulfonate by
RT defined pairs of heterotrophic bacteria.";
RL Appl. Environ. Microbiol. 70:4053-4063(2004).
RN [2] {ECO:0000313|Proteomes:UP000000784}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14801 / SPH-1 {ECO:0000313|Proteomes:UP000000784};
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL Submitted (NOV-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:ARBA00033635,
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};
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DR EMBL; CP000884; ABX35136.1; -; Genomic_DNA.
DR AlphaFoldDB; A9BZ36; -.
DR STRING; 398578.Daci_2498; -.
DR KEGG; dac:Daci_2498; -.
DR eggNOG; COG2609; Bacteria.
DR HOGENOM; CLU_009154_2_0_4; -.
DR OMA; LVFFQPH; -.
DR Proteomes; UP000000784; Chromosome.
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}; Pyruvate {ECO:0000256|PIRNR:PIRNR000156};
KW Reference proteome {ECO:0000313|Proteomes:UP000000784};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 136..337
FT /note="Transketolase signature 1"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 527..739
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT DOMAIN 766..811
FT /note="Transketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02780"
FT BINDING 271
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 303
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 902 AA; 98079 MW; 337C187B8B271E75 CRC64;
MKCWNMAFSL SMNGCSCRPA SPKVADMNAP TPLAALADID TDPQETAEWR EAFLALVATE
GPQRARFVLA ELARMAREQR LGWQPDLNTP YVNSVAAQQQ PVFPGDLAIE ERLASIMRWN
ALAMVVRANQ AYGELGGHIA SYASAADLFE TGFNHFFHAR EGLEPGQHRG DLVFFQPHSA
PGVYARAFLE GRLTEQDLQH YRQEISAPAA GAQGLSSYPH PWLMPDFWQF PTGSMGIGPI
SSIYHARFMR YLTHRRLLDC QERKVWGVFG DGEMDEPESM SALTLAAREG LDNLVWVVNC
NLQRLDGPVR GNGRIVDELE RLFAGAGWNV VKLLWGSDWD GLFARDLTGT LARTLGGTVD
GQMQTFAAND GRYNREHFFG QNPELAALAQ GLTDEQIDRL KRGGHDLVKI HAAYAAAAAH
RGQPTVILAH TKKGYGMGSA GQGKMTTHSQ KKLDESDLIE FRNRFNLPLS DEQAKGLAFH
KPADDSAEMQ YLRDRRTALG GALPRRETVC DRVPVPALEQ YAQFALAPAG KEMSTTMAFV
RMLGGLLKDA QLGPRIVPIV ADEARTFGMA NLFKQVGIYS SLGQRYAPED IGSVLSYREA
LDGQILEEGI SEAGAIASWT AAATSYSVHG LAMLPFYIYY SMFGFQRVGD AIWAAADQRA
RGFLLGATSG RTTLGGEGLQ HQDGSSHLVA ATIPNCKAWD PAHAGELAVI LDAGMREMLV
EQRDVFYYIT LMNENYAQPD LPQGAAEGVL RGGYVFGRFG DAGHATQHVT LLGSGAILTE
VLKAAEQLAS EGMAATVVSV TSWSELARDG VACEQRMLAG EAPGQPWIAQ LLDGTQGPVI
AATDYVRAVP ETVRAFLPAG RRFLTLGTDG FGRSDTRAAL RGHFGVDAHS VAQAARRCSQ
AA
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