ID A0A1H5RAC3_9PSEU Unreviewed; 931 AA.
AC A0A1H5RAC3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=SAMN05421837_10823 {ECO:0000313|EMBL:SEF35362.1};
OS Amycolatopsis pretoriensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=218821 {ECO:0000313|EMBL:SEF35362.1, ECO:0000313|Proteomes:UP000198878};
RN [1] {ECO:0000313|EMBL:SEF35362.1, ECO:0000313|Proteomes:UP000198878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44654 {ECO:0000313|EMBL:SEF35362.1,
RC ECO:0000313|Proteomes:UP000198878};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNUJ01000008; SEF35362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5RAC3; -.
DR STRING; 218821.SAMN05421837_10823; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000198878; 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:SEF35362.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 160..327
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 508..735
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 256
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 288
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 931 AA; 102743 MW; 144EFBBF8565FFC5 CRC64;
MAPQNDGASG KETPARVRVI RDGLAAHLPD IDPEETAEWL DSFDEALARG GQQRARYLML
RILERARERN VGVPALTSTD YVNTIPTENE PWFPGDEEIE RRYRAYIRWN AAIMVHRAQR
PGVGVGGHIS TYASSAALYE VGFNHFFRGK DHSGGGDQIY IQGHASPGIY ARAFLEGRLS
ESQLDGFRQE FSHAGEGGGL PSYPHPRLMP EFWENPTVSM GLGPMNAIYQ ARFNRYLRDR
GIKNTDDQHV WAFLGDGEMD EAESRGLVHV AAGEGLDNLT FVINCNLQRL DGPVRGNGKI
IQELESYFRG AGWNVIKVIW GREWDSLLHA DRDGALVNLM NVTPDGDYQT YKANDGAFVR
EHFFGRDPRT KDLVKDLSDA DIWNLKRGGH DYRKVYAAYK SALEHHGQPT VILAHTIKGY
GLGPAFEGRN ATHQMKKLTL DDLKLFRDSQ RIPISDEELE RDPKLPPYYH PGANSPEIEY
LIGRRKALGG FLPERRPKAA KALVLPGDKV YEGIRKGSGK QEVATTMAFV RLVRELAKDS
EIGKRVVPII PDEARTFGLD SMFPTAKIYN PHGQTYTSVD ASLMLAYKES EKGQLLHEGI
NEAGSTASFT AVGTSYATHG EPMIPIYIFY SMFGFQRTGD GLYAAADQMA RGFVLGATAG
RTTLTGEGLQ HADGHSLLLA ATNPAAVAYD PAWSFEIAHI VKDGLRRMYG ETGPDGNGEN
VFYYMTIYNE PYQQPAEPEN LDVDGLLKGL YKYADAPSGD GPEVQILVSG VTMPDALKAQ
KLLSEEWGVR AAVWSATSWT ELRREAVEID HDNLLYPGSE PRVPFVTEKL QGANGPVVAV
SDWMRAVPDL IRPYVPTDML TLGTDGFGFS DTRPAARRKF LVDAESITVG ALSILAKRGE
VDQAKVLEAA TKYRLDDIAA AGPQTSDSGS A
//
