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Database: UniProt
Entry: A9BZ36_DELAS
LinkDB: A9BZ36_DELAS
Original site: A9BZ36_DELAS 
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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