ID A0A239BRD0_9ACTN Unreviewed; 932 AA.
AC A0A239BRD0;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN04488107_1374 {ECO:0000313|EMBL:SNS10209.1};
OS Geodermatophilus saharensis.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Geodermatophilus.
OX NCBI_TaxID=1137994 {ECO:0000313|EMBL:SNS10209.1, ECO:0000313|Proteomes:UP000198386};
RN [1] {ECO:0000313|EMBL:SNS10209.1, ECO:0000313|Proteomes:UP000198386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45423 {ECO:0000313|EMBL:SNS10209.1,
RC ECO:0000313|Proteomes:UP000198386};
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; FZOH01000002; SNS10209.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239BRD0; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000198386; Unassembled WGS sequence.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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:SNS10209.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 162..322
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 503..735
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 287
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 932 AA; 104052 MW; 6492C05FABD72018 CRC64;
MSSPQQGGDP TRDAGQPRAV ITDGLPSQLV DTDPDETQEW VESLDSVVEH AGRGRARYLM
LKMLQRSREQ QVGVPALRST DYINTIPPER EPYFPGDEDT ERRIRAYIRW NAAIMVHRAQ
RPGIAVGGHI SSYASSASLY EVGFNHFFRG KDHPGGGDQI WFQGHASPGI YARAFLEGRL
TEHQLDGFRQ EVSHPGGGLS SYPHPRLMPD FWEFPSVSMG LGPMNAIYQA RFNRYLHSRG
IKDTSDQHVW AFLGDGEMDE PESLGLIGLA AREELDNLTF VVNCNLQRLD GPVRGNGKVI
QELESFFRGA GWNVIKVIWG REWDPLLAAD RDGALVNLMN QTPDGDYQTY KAEDGAYVRE
HFFGRDPRTR KLVENMSDKE VWDLSRGGHD YRKVYAAFKA AVEHRGQPTV ILAKTIKGWT
LGSHFEGRNS THQMKKLTAE DLAAFRDRLY LPIPDEALDK TLPPYYKPDP DSDEMQYMLE
RRRALGGAVP RRRAEFKTLK APDDKALDVL RRGSGKQEVA TTMAFVRLLK ELLKDKELGP
RFVPIIPDEA RTFGMDSLFP SQKIYNPGGQ RYTSVDRELM LAYRESEQGQ ILHEGINEAG
STASFTAAGT SYATHGEPMI PIYIFYSMFG FQRTGDSFWA AADQMTRGFV LGATAGRTTL
NGEGLQHEDG HSLLLAHTNP AVVSYDPAFS YEVGHITRDA LVRMYGEDPG APLGGHRSPD
VMYYLTVYNE PYNQPAEPEG LDVQGLLAGM YLYAPGQGEG PRAQVLASGV AVPWALRAQE
LLREDWGVVA DVWSVTSWTE LRRQADEVSE RNFLHPEEEP QVPYVTERLR GTDGPVVAVS
DWMRSVPDLI APYVPGGMAT LGTDGFGLSD TRPALRRHFH VDAESVVVRT LGALADRGEI
DRAKVREAVE RYRIRDVQAA PADERSDPSP AT
//
