ID A0A068NFA2_9ACTO Unreviewed; 920 AA.
AC A0A068NFA2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=FB03_01215 {ECO:0000313|EMBL:AIE82117.1};
OS Actinotignum schaalii.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Actinotignum.
OX NCBI_TaxID=59505 {ECO:0000313|EMBL:AIE82117.1, ECO:0000313|Proteomes:UP000035032};
RN [1] {ECO:0000313|EMBL:AIE82117.1, ECO:0000313|Proteomes:UP000035032}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 27420 {ECO:0000313|EMBL:AIE82117.1,
RC ECO:0000313|Proteomes:UP000035032};
RX PubMed=25189588;
RA Kristiansen R., Dueholm M.S., Bank S., Nielsen P.H., Karst S.M.,
RA Cattoir V., Lienhard R., Grisold A.J., Olsen A.B., Reinhard M., Soby K.M.,
RA Christensen J.J., Prag J., Thomsen T.R.;
RT "Complete Genome Sequence of Actinobaculum schaalii Strain CCUG 27420.";
RL Genome Announc. 2:e00880-14(2014).
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; CP008802; AIE82117.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A068NFA2; -.
DR KEGG; asg:FB03_01215; -.
DR Proteomes; UP000035032; 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:AIE82117.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 152..312
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 498..724
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 920 AA; 102580 MW; E667259609BE2350 CRC64;
MASQDSDDRM VSGQLSQIPD VDPEETREWL ASVDDLIETN GADRARFILA SVDEHARAKG
VSVSPDLVTP YINTIPAEEE PPYPGTPEEE ELEHQFRSWT RWNAAVMVTR AQRPGVGVGG
HISSYAAQAT LYEVGFNHFF RGPDAPGGGD QIFFQGHSSP GNYARAYLEG RLTEADLDSF
RQEASHISGG RGLPSYPHPH QMPDFWQFPT VSLGLGATNS IYQAWFNRYL SERGIKDTSD
SHVWAFLGDG EMDEPESRGM LQLAASQKLD NLTWVVNCNL QRLDGPVRGN GNIVQELESF
FKGAGWNVIK VLWGSGWDKL LAQDKDHALV DLMTSTPDGD YQGFKANDGS YVRNNFFGRD
PRTKAMVEDW SDDEIWALRR GGHDHHKIYA AYRAALAHKG QPTVILAQTV KGYDLGSNFA
GRNATHQMKK LNSNDLKLLR DTLRIPIDDS QLEDPYNAPY YKPAEDHPAM KHMRERREAL
GGYLPQRRTH QGGIALPADK PFQSMKKGSG KQKVATTMAL VRLLKDIMRD KEFGFRMVPI
VPDEARTFGM DSMFPSAKIF NTQGQQYTAV DHDMLLSYKE STQGQLLHTG ITEAGSLSAF
VAAGTSYATH NTPMVPFYIF YSMFGFQRTG DQFWAAYDQL ARGFIIGGTA GRTTLTGEGS
QHMDGHSPVL ASTNPGMVIY DAAYAYELGH IFKDGLKRMY GDGSDGREQN VMYYLTVYNE
PIHQPAEPEN VDVDGIIRGI YKLDEADGLG GPRVNLLSSG VGVRWAREAK RMLRDDWGVD
ATVYSVTSWY ELRKDGLATN EYNYLHPEEE PRKAYVTAKL EGEEGPFIAT SDFEHQVQDS
IREWIPGDYE TLGAKGIGIS DTRPAARRYF KIDDATMVVR ALYALAKAGK IDRSVVRQAI
EKYDLHNPAA AEPVPDNDPE
//
