ID A0A1L7FED1_9PSEU Unreviewed; 930 AA.
AC A0A1L7FED1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=UA75_25930 {ECO:0000313|EMBL:APU23159.1};
OS Actinoalloteichus sp. GBA129-24.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Actinoalloteichus.
OX NCBI_TaxID=1612551 {ECO:0000313|EMBL:APU23159.1, ECO:0000313|Proteomes:UP000185506};
RN [1] {ECO:0000313|EMBL:APU23159.1, ECO:0000313|Proteomes:UP000185506}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GBA129-24 {ECO:0000313|EMBL:APU23159.1,
RC ECO:0000313|Proteomes:UP000185506};
RA Ruckert C., Nouioui I., Willmese J., van Wezel G., Klenk H.-P.,
RA Kalinowski J., Zotchev S.B.;
RT "Complete genome sequence of Actinoalloteichus fjordicus DSM 46856
RT (=GBA129-24).";
RL Submitted (JUN-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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP016077; APU23159.1; -; Genomic_DNA.
DR RefSeq; WP_075742499.1; NZ_CP016077.1.
DR AlphaFoldDB; A0A1L7FED1; -.
DR STRING; 1612551.UA75_25930; -.
DR KEGG; acti:UA75_25930; -.
DR Proteomes; UP000185506; Chromosome.
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:APU23159.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 159..323
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 507..734
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 930 AA; 103251 MW; D69BA36F1C9F1ABA CRC64;
MAPQNNGNAA DNAPQRVRVI RDGLAAHLPD IDPEETAEWL ESFDSILSAT GRQRARYVML
RLLERARESG VGLPSLTSTD YVNSIPTDVE PWFPGDEETE RRYRAWIRWN AAMTVHRAQR
PGIGVGGHIS TYASSATLYE VGFNWFFRGK DHPGGGDQVF IQGHGSPGIY ARAFLEGRLT
ESQLDGFRQE YSHAGPGGGL PSYPHPRLMP HFWEFPTVSM GLGPMNAIYQ ARFNRYLHNR
GIKDTSDQHV WAFLGDGEMD EPESRGLIHV AANEGLDNLT FVINCNLQRL DGPVRGNGKI
IQELESYFRG AGWNVIKVVW GREWDSLLHG DRDGALINLM NTTPDGDYQT YKANDGAYVR
EHFFGRDPRT KELVTEYTDQ QIWNLKRGGH DYRKVYAAYQ AATSHHGQPT VILAKTIKGY
GLGPTFAGRN ATHQMKKMTL NDLKLFRDST RVPITDAQLE ADPYLPPYYH PGNDAPEIQY
LLDRRRRLGG FVPERRVKAK PLVLPGDKVY DVVKRGSGKQ DVATTMAFVR LIRDLAKDPE
IGPRLVPIIP DEARTFGMDS MFPTQKIYNP SGQLYTSVDA QLMLAYKESE QGQILHEGIN
EGGSTASFTA AATSYATHGE HMIPVYIFYS MFGFQRTGDG LWAAADQMAR GFVLGATAGR
TTLTGEGLQH NDGHSLLLAA TNPAVVSYDP AWSFEVAHIV KDGLRRMYGE SEEFPHGEDV
MFYLTVYNDP YRQPAEPDDL DVDGLLRGLY RYAKAPAGDG PTAQILASGV SMPWALRAQE
LLAEHHGVQA AVWSATSWAE LRREAVRTEQ DNLLRPGSRR EVPHVTRALE GTGGPVVAVS
DWMRAVPDLI RPWVPTDMLT LGTDGFGFSD TRPAARRKFL VDAESIVVGT LLALARRGDI
DHSVAEQAAR TYRIEDVQAA GPQTSDPGVS
//
