ID D5CPH6_SIDLE Unreviewed; 887 AA.
AC D5CPH6;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
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=Slit_2746 {ECO:0000313|EMBL:ADE12971.1};
OS Sideroxydans lithotrophicus (strain ES-1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Gallionellaceae; Sideroxydans.
OX NCBI_TaxID=580332 {ECO:0000313|EMBL:ADE12971.1, ECO:0000313|Proteomes:UP000001625};
RN [1] {ECO:0000313|EMBL:ADE12971.1, ECO:0000313|Proteomes:UP000001625}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES-1 {ECO:0000313|EMBL:ADE12971.1,
RC ECO:0000313|Proteomes:UP000001625};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Munk A.C., Detter J.C., Han C., Tapia R., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Emerson D., Woyke T.;
RT "Complete sequence of Sideroxydans lithotrophicus ES-1.";
RL Submitted (MAR-2010) 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|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; CP001965; ADE12971.1; -; Genomic_DNA.
DR RefSeq; WP_013030869.1; NC_013959.1.
DR AlphaFoldDB; D5CPH6; -.
DR STRING; 580332.Slit_2746; -.
DR KEGG; slt:Slit_2746; -.
DR eggNOG; COG2609; Bacteria.
DR HOGENOM; CLU_009154_2_0_4; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000001625; 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: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}; Pyruvate {ECO:0000256|PIRNR:PIRNR000156};
KW Reference proteome {ECO:0000313|Proteomes:UP000001625};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 137..295
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 474..699
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 887 AA; 99666 MW; D9EEDFD59CD2E901 CRC64;
MATQQPPKVD QDPQETQEWL DALQSVLDKE GAERAHFLMD QLIHHARMAG DDMPISATTP
YINTIPLDKE ERSAGNFELE HRIRALMRWN AMAIVMNANK ESSELGGHIA SFASAATLYD
VAFNHFFHGK TDEHGGDLVY FQGHSSPGIY ARAFLEGRLS EEQLYKFRQE VDGGGLSSYP
HPWLMPDFWQ FPTVSMGLGP LMAIYQARFM RYLQHRELAQ TNGRKVWAFL GDGETDEPES
LGAISMAGRE KLDNLIFVIN CNLQRLDGPV RGNGKIIQEL EGVFRGAGWN VIKVIWGRWW
DRLLAKDKTG LLLKRMEEVV DGEYQTYKSK DGAYVRQHFF GKYPELLELV ADMSDDEIWH
LNRGGHDPFK VFAAYAAACK HKGQPTVILA KTVKGYGMGE AGEGQNPTHQ QKKIGEDALR
RFRDRFNIPV TDEQLTQLPF VRPAEDSQEM KYLRERGAAM GTLPARKPIV KKLQIPDLPA
FDALLKDSEG REFSTTMAFV RLLGVLVKDK NIGKKIVPIV PDESRTFGME GMFRQLGIFS
QVGQLYTPQD ADQLMFYKES EAGQILQEGI NEAGGMADWI AAATSYASHD VAMIPFYIYY
SMFGFQRIGD LAWAAGDMRA RGFLVGGTAG RTTLNGEGLQ HQDGHSHLQA AMIPNCVSYD
PTFAYELAVI VQDGMRRMYQ NQEDVFYYLT VMNENYAHPA MPKGVEAGII KGMYKFSASK
AKTKAKVQLL GSGTILREVI AAGELLERDF GIAADVWSVT SFNELRREGI DCERWNTLHP
EAKARVSYVE QSLDAKTPVI AATDYIRSYA DQIRPFVKAR YKTLGTDGFG RSDFRVKLRQ
FFEVDRFYVA VTALKALADE GTIPASEVSK AIKLYKINPD KPNPTTV
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