ID A0A239LZV6_9ACTN Unreviewed; 916 AA.
AC A0A239LZV6;
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=SAMN05421812_1058 {ECO:0000313|EMBL:SNT36036.1};
OS Asanoa hainanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Asanoa.
OX NCBI_TaxID=560556 {ECO:0000313|EMBL:SNT36036.1, ECO:0000313|Proteomes:UP000198362};
RN [1] {ECO:0000313|EMBL:SNT36036.1, ECO:0000313|Proteomes:UP000198362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5593 {ECO:0000313|EMBL:SNT36036.1,
RC ECO:0000313|Proteomes:UP000198362};
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; FZPH01000005; SNT36036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239LZV6; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000198362; 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:SNT36036.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198362};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 128..313
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 500..715
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 246
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 278
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 916 AA; 101993 MW; 0DCB35D8F5662897 CRC64;
MATERKRPVI SDGLPSQLPD IDPEETAEWV ESLDGVIDAG GAKRARYVML RLLERARERN
VGVPPLTTTD YINTIPPERE PWFPGDEFVE RRIRAYIRWN AAMLVHRAQR PEIGVGGHIS
TYASAAALYE VGFNHFFRGK SHPGGGDHIF YQGHASPGMY ARAFMEGRLS EERLDGFRQE
LSHAGLGGGL PSYPHPRLMP DFWEFPTVSM GLGGMNAIYQ ARFNRYLHNR GIKDTSDQHV
WAFLGDGEMD EPESLGAIGV AAREELDNLT FVINCNLQRL DGPVRGNGKV MQELEAFFRG
AGWNVIKVVW GREWDPLLAA DSDGALVNLM NTTPDGDYQT YKAESGAYVR EHFFGRDPRT
RKMVEGMTDD EIWNLKRGGH DYRKIYAAYK AATEHTGQPT VILAKTIKGW TLGSSFEGRN
ATHQMKKLTL DDLKSFRDRL YLDIPDKALE ENPYLPPYIR PEDKSDEMEY LHERRRALGG
YLPSRNTKVI PLQIPGSERF GDVKRGSGKQ KIATTMAFVR LLKDIMKDRE FGKRWVPIIP
DEARTFGMDS LFPTAKIYSP HGQNYTPVDR ELFLSYKEAL GGQILHEGIN EAGSVASFTA
AGTSYATHGE PMIPLYIFYS MFGFQRTGDG FWAAADQMAR GFVLGATAGR TTLNGEGLQH
EDGHSHLIAA TNPAVVAWDP AFAFEMAHIV ERGLHRMYGE EAENVFYYMT IYNEPILQPV
EPVDLDVEGL LKGIYRYSPA PAVDGGGIKA NILASGTGMQ WALKAQQLLA QDWGVAADVW
SVTSWTELRR DAVQAEEYNL LHPGSEPRVP YIRRKLAGSD GPVIAVSDFM RAVPDLISRW
IPGDYTSLGT DGFGLSDTRH ALRRHFNVDA ESVAVATLRQ LAVRGEVAPS IPVEAARKYA
IDDVNAAPVG ETGGDS
//
