ID A0A177YPY5_9NOCA Unreviewed; 943 AA.
AC A0A177YPY5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=A3K89_00425 {ECO:0000313|EMBL:OAK57320.1};
OS Rhodococcus kyotonensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=398843 {ECO:0000313|EMBL:OAK57320.1, ECO:0000313|Proteomes:UP000077519};
RN [1] {ECO:0000313|EMBL:OAK57320.1, ECO:0000313|Proteomes:UP000077519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KB10 {ECO:0000313|EMBL:OAK57320.1,
RC ECO:0000313|Proteomes:UP000077519};
RA Jeong H., Hong C.E., Jo S.H., Park J.M.;
RT "Genome sequence of Rhodococcus kyotonensis KB10.";
RL Submitted (MAR-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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAK57320.1}.
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DR EMBL; LVHI01000001; OAK57320.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177YPY5; -.
DR Proteomes; UP000077519; 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:OAK57320.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077519};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 170..338
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 514..747
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 297
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 299
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 943 AA; 104550 MW; 6212A3F74DB64714 CRC64;
MSELNKDERQ TTHAAGKTSG PTGSDGRVRV IREGVASYLP DIDSSETDEW IESFDGLLER
SGPARARYLM LRLLERAGER RVALPSLTST DYVNTIPTEN EPWFPGDEEV ERRYRAWIRW
NAAIMVHRAQ RPGVGVGGHI STYASSAALY EVGFNHFFRG KDHPGGGDQI FIQGHASPGI
YARAFLEGRI PAERMDGFRQ EYSHSDQGGG LPSYPHPRLM QDFWEFPTVS MGLGPMNAIY
QARFNHYLHD RGIKDTSDQH VWAFLGDGEM DEPESRGLAH VAATEGLDNL TFVVNCNLQR
LDGPVRGNGK IIQELESFFR GAGWNVIKVI WGREWDSLLH ADKDGALVNL MNVTPDGDYQ
TYKANDGGYV RDHFFGRDPR TKELVKDLSD DDIWNLKRGG HDYRKVHAAY AAAMAHKGQP
TVILAHTIKG YTLGKSFEGR NATHQMKKLT LDDLKKFRDL QHIPISDEEL EKDPYLPPYY
HPGPDAPEIQ YMLERRKNLG GFVPERRTSP KPLPQPKDDT YKTLLKGSGK QEVATTMALV
RVMKELLRDK EIGHRIVPII PDEARTFGMD SWFPSLKIYN RNGQLYTSVD SELMLAYKEN
ATGQILHEGI NEAGSTSSFT AVGTSYATHG EPMIPLYIFY SMFGFQRTGD GLWAAADQMA
RGFVLGATAG RTTLTGEGLQ HADGHSLLLA ATNPAAVAYD PAFSYEIAHI VKDGLRRMYG
GTEGTEGFGG ENIFYYITLY NEPYQQPAQP EDLDVDALLK GIYLFEKPQQ GDGPEAQILA
SGVGLVSARK ARQLLEDEWG VRSGVWSVTS WSELRRDGVE AEQEALRNPG AEKRVPFVTQ
ALSAAAGPVV AASDWMRAVP DQIRQWVPGD YVTLGTDGFG FSDTRPAARR VFNVDAESIV
VAVLTALGES GEIDKSKAVD AAAKYRIDDV HAAETSYADT GSA
//
