ID A0A239HDD5_9BACT Unreviewed; 896 AA.
AC A0A239HDD5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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 ORFNames=SAMN05421770_102354 {ECO:0000313|EMBL:SNS79380.1};
OS Granulicella rosea.
OC Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC Granulicella.
OX NCBI_TaxID=474952 {ECO:0000313|EMBL:SNS79380.1, ECO:0000313|Proteomes:UP000198356};
RN [1] {ECO:0000313|EMBL:SNS79380.1, ECO:0000313|Proteomes:UP000198356}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18704 {ECO:0000313|EMBL:SNS79380.1,
RC ECO:0000313|Proteomes:UP000198356};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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|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; FZOU01000002; SNS79380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239HDD5; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000198356; 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: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};
KW Pyruvate {ECO:0000256|PIRNR:PIRNR000156, ECO:0000313|EMBL:SNS79380.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198356};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 147..311
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 491..709
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 272
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 896 AA; 99621 MW; E2EC451210CA3E2E CRC64;
MSTKLEIAAS TQNRTPAEKQ DIAAEVAEWI EAFDQVVAQD WEIGADLLKA LRQRANEAGV
PVAGSVTTPY KNTIPKHDEV PYPGDRNLER RVEALIRWNA MAMVHKQNKY DAGIGGHIST
YSSQCTLLEV GFNHFFRASY GSEPGDFIYF QGHASPGVYS RAFLEGRLTE DHLHNFRHEL
RDTPGLSSYP HPWLMQDFWQ FPTVSMGIGP LNAIYQARFM RYLENRGLIE KTGRKVWAFV
GDGETDEVDT LGAISLGARE KLDNLIFVVN CNLQRLDGPV RGNARIIDEL EAVFRGANWN
VIKVLWGSDW DELFALDHTG LLLKRMEECV DGDYQRFKAK DGAYLREHFF GKYPELLKIV
EHKTDEELAH LHRGGHDPIK IYNAYKRAVE HKGGPTVILA HTVKGYGIAS AQSRNPTHSE
KKLTDEGLAA FVKRFDIPLP ETAALNADFY KPADDDAALQ YLHAHRAALG GYLPKREIPA
KNFDAPAIDF FKGWLGGSGS RAISTTMGFV NMLNGMLKHP EIGKLIVPII PDEGRTFGFE
SVMKAVGIYA PEGQKYIPHD ADMLLSYNEK KNGQILEEGI TEAGSMASFT AAGTAYTNYR
VPTVPFYLYY SMFGFQRIGD MAWAFADSRG KGFLMGGTAG RTTMLGEGLQ HQDGHSPVLS
GTVPTCITYD PAFVYEMAVI VQDGLRRMYQ EGENVFYYLT MYNEDYLQPA MPEGVTEGIL
KGLYKYQPAA GTAVAQLFGS GPILNEVVKA QGILAEKYGV HADVWSVPSY NEVRREALSV
ERWNRLHPAE PERKSYLATL LDGTAGPIIA ASDYMKSLPD ALSPWLQSRL VTLGTDGFGR
SDNREHLRRH FEVSAEAIVG ATLSKLAREG SFDPKAAQQA FADLGLDTEI KDPARA
//
