ID A0A1A3R155_9MYCO Unreviewed; 929 AA.
AC A0A1A3R155;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=A5655_21985 {ECO:0000313|EMBL:OBK52393.1};
OS Mycobacterium sp. 1081908.1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834066 {ECO:0000313|EMBL:OBK52393.1, ECO:0000313|Proteomes:UP000092324};
RN [1] {ECO:0000313|Proteomes:UP000092324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1081908.1 {ECO:0000313|Proteomes:UP000092324};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Garcia-Basteiro A.,
RA Lopez-Varela E., Palencia S.;
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 -!- 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:OBK52393.1}.
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DR EMBL; LZLY01000022; OBK52393.1; -; Genomic_DNA.
DR RefSeq; WP_067005879.1; NZ_LZLY01000022.1.
DR AlphaFoldDB; A0A1A3R155; -.
DR STRING; 1834066.A5655_21985; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000092324; 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:OBK52393.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 165..331
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 512..733
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 290
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 292
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 929 AA; 103128 MW; 76F64376A739EDAC CRC64;
MTTEFARHDL AKTPSSASEP DRVRVIREGV ASYLPDIDPD ETSEWLESFD EMLERSGPAR
ARYLMLRLLE RAGDQRVAIP SLTSTDYVNT IPTELEPWFP GDEDVERRYR AWIRWNAAIM
VHRAQRPGIG VGGHISTYAS SAALYEVGFN HFFRGKSHPG GGDQVFIQGH ASPGIYARAF
LEGRLSEERL DGFRQEHSHA GGGLPSYPHP RLMPDFWEFP TVSMGLGPLN AIYQARFNHY
LHDRGIKDTS DQHVWCFLGD GEMDEPESRG LAHVGALEGL DNLTFVINCN LQRLDGPVRG
NGKIIQELES FFRGAGWNVI KVVWGREWDA LLHADKDGAL VNLMNTTPDG DYQTYKANDG
AYVRDHFFGR DPRTKALVEQ MTDSEIWNLK RGGHDYRKVY AAYRAAVDHK GQPTVILAKT
IKGYSLGAHF QGRNATHQMK KLALQDLKDF RDAIRIPISD AQLEEDPYLP PYYHPGPDAP
EIRYLLDRRR ALGGFLPERR TKAKALSLPG RDTYAALKKG SGNQEVATTM ATVRTFKEVL
RHKEVGPRIV PIIPDEARTF GMDSWFPSLK IYNRLGQLYT AVDAELMLAY KESEVGQILH
EGINEAGSVG SFIAAGTSYA THNEPMIPIY IFYSMFGFQR TGDGLWAAAD QMARGFLLGA
TAGRTTLTGE GLQHADGHSL LLAATNPAVV SYDPAFAFEI AYIVESGLAR MFGENPENVF
FYITVYNEPY PQPPEPDNFD PEGVLRGIYR YRAATEQRAN KAQILASGVA MPSALQAADM
LAAEWDVAAD VWSVTSWGEL NRDGVSVERA RLRHPDQPAG TPYVTRALAD AAGPVIAVSD
WMRAVPEQIR QWVPGTFVTL GTDGFGFSDT RPAARRYFNT DAESQVVAVL EALARDGEID
PSVPVAAARE YRIDDVLAAP EQTSDPGVA
//
