ID A0A0Q8VCA3_9MICO Unreviewed; 908 AA.
AC A0A0Q8VCA3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=ASE16_08820 {ECO:0000313|EMBL:KRC51031.1};
OS Leifsonia sp. Root227.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736496 {ECO:0000313|EMBL:KRC51031.1, ECO:0000313|Proteomes:UP000051819};
RN [1] {ECO:0000313|EMBL:KRC51031.1, ECO:0000313|Proteomes:UP000051819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root227 {ECO:0000313|EMBL:KRC51031.1,
RC ECO:0000313|Proteomes:UP000051819};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC51031.1, ECO:0000313|Proteomes:UP000051819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root227 {ECO:0000313|EMBL:KRC51031.1,
RC ECO:0000313|Proteomes:UP000051819};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KRC51031.1}.
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; LMIO01000002; KRC51031.1; -; Genomic_DNA.
DR RefSeq; WP_055893781.1; NZ_LMIO01000002.1.
DR AlphaFoldDB; A0A0Q8VCA3; -.
DR STRING; 1736496.ASE16_08820; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000051819; 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}; Pyruvate {ECO:0000256|PIRNR:PIRNR000156};
KW Reference proteome {ECO:0000313|Proteomes:UP000051819};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 144..305
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 489..714
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 271
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 908 AA; 100748 MW; 50D70ECE4198D130 CRC64;
MTVNDQDPYS VNHIDSDPEE TAEWQESLDA LVAAHGHERA REIMLSLLKR SKELQLGVPM
VPTTDYINTI SPENEPDFPG DEEVERRYRA WIRWNAAVMV HRAQRPGIAV GGHLSSYASS
ATLYEIGFNH FFRGQDHPGG GDQIFFQGHA SPGPYARAFL EGRLSADQLD GFRQEKSHAG
GGLSSYPHPR LMPEFWQFPT VSMGLGPINA IYQAQLNKYL TNRGIKDASD QHVWAFLGDG
EMDEVESRGQ LQVAANEKLD NLTFVVNANL QRLDGPVRGN GKIIQELESY FRGAGWNVIK
VIWGREWDDL LARDSDGALV NLMNQTPDGD YQTYKTENGA YVRENFFGRD PRTLELVKDY
TDDQVWGLKR GGHDYRKVYA AFKAATEHKG QPTVIIAKTI KGYGLGPSFE GRNATHQMKK
MTLDNLKTFR DAMRIPVSDA QLEENPYLPP YYNPGPEDEA IQYLHDRRRA LGGYVPERRS
KYTQLNLPDD SAYAISKKGS GTQEIATTMA FVRLLKDLLR AKDFGHRIVP IIPDEARTFG
MDAFFPNAKI YNPNGQHYTS VDRELLLAYK ESPQGQIIHV GINEAGALAA FTNVGTSYAT
QGEPLIPVYV FYSMFGFQRT GDAIWAAGDQ MARGFMIGAT AGRTTLTGEG LQHADGHSLV
LANTNPAVVS YDPAYGYEIG HIVRSGLERM YGGNHPDPNV MYYLTVYNEP IVHPAEPEGV
DVDGIVRGIH RLSVSDVSGP KAQLLASGVS VPWALEAQHL LAQDWGVSAD VWSVTSWSEL
RRDGLAAEEH NFLYPQQEKQ VPYVTRKLQD ADGPFVAVTD FMHAVPDQIR QFVPGEFATL
GADGFGFSDT RPAARRFFKI DGPSMVVRTL ELLAARGQVD PNAPAWAIEK YLLHDVNAGT
TGSAGGES
//
