ODP1_MYCTU
ID ODP1_MYCTU Reviewed; 930 AA.
AC P9WIS9; L0TBX6; Q10504;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 07-JAN-2015, sequence version 2.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000305|PubMed:16045627};
DE Short=PDH E1 component {ECO:0000305};
DE EC=1.2.4.1 {ECO:0000269|PubMed:16045627};
GN Name=aceE; OrderedLocusNames=Rv2241; ORFNames=MTCY427.22;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP PROTEIN SEQUENCE OF 8-55, AND SEQUENCE REVISION TO N-TERMINUS.
RC STRAIN=H37Rv;
RX PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT annotated encoding genes.";
RL Genomics 114:292-304(2022).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP IDENTIFICATION IN THE PDH COMPLEX.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=16045627; DOI=10.1111/j.1365-2958.2005.04741.x;
RA Tian J., Bryk R., Shi S., Erdjument-Bromage H., Tempst P., Nathan C.;
RT "Mycobacterium tuberculosis appears to lack alpha-ketoglutarate
RT dehydrogenase and encodes pyruvate dehydrogenase in widely separated
RT genes.";
RL Mol. Microbiol. 57:859-868(2005).
RN [4]
RP PUPYLATION AT LYS-375, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=20066036; DOI=10.1371/journal.pone.0008589;
RA Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E.,
RA Gygi S.P., Darwin K.H.;
RT "Prokaryotic ubiquitin-like protein (Pup) proteome of Mycobacterium
RT tuberculosis.";
RL PLoS ONE 5:E8589-E8589(2010).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex, that
CC catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
CC AceE has reductase activity with pyruvate but does not react with 2-
CC oxoglutarate. {ECO:0000269|PubMed:16045627}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + H(+) + pyruvate = (R)-N(6)-(S(8)-
CC acetyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + CO2; 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:0000269|PubMed:16045627};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:16045627};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000269|PubMed:16045627};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=47 uM for pyruvate {ECO:0000269|PubMed:16045627};
CC pH dependence:
CC Optimum pH is 8.0 for PDH complex activity. Half-maximal activity is
CC observed at pH 7.0 and pH 9.0. Activity is abolished at pH < 5.
CC {ECO:0000269|PubMed:16045627};
CC -!- SUBUNIT: Homodimer (By similarity). Part of the PDH complex, consisting
CC of multiple copies of AceE (E1), DlaT (E2) and Lpd (E3). {ECO:0000250,
CC ECO:0000269|PubMed:16045627}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP45021.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
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DR EMBL; AL123456; CCP45021.1; ALT_INIT; Genomic_DNA.
DR PIR; E70778; E70778.
DR RefSeq; NP_216757.3; NC_000962.3.
DR RefSeq; WP_003911788.1; NZ_NVQJ01000008.1.
DR AlphaFoldDB; P9WIS9; -.
DR SMR; P9WIS9; -.
DR STRING; 83332.Rv2241; -.
DR PaxDb; P9WIS9; -.
DR PRIDE; P9WIS9; -.
DR DNASU; 887246; -.
DR GeneID; 45426221; -.
DR GeneID; 887246; -.
DR KEGG; mtu:Rv2241; -.
DR PATRIC; fig|83332.12.peg.2499; -.
DR TubercuList; Rv2241; -.
DR eggNOG; COG2609; Bacteria.
DR SABIO-RK; P9WIS9; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0045254; C:pyruvate dehydrogenase complex; IDA:MTBBASE.
DR GO; GO:0000287; F:magnesium ion binding; IDA:MTBBASE.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IDA:MTBBASE.
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 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 PANTHER; PTHR43825:SF3; PTHR43825:SF3; 1.
DR Pfam; PF17831; PDH_E1_M; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR SUPFAM; SSF52518; SSF52518; 2.
DR SUPFAM; SSF52922; SSF52922; 1.
DR TIGRFAMs; TIGR00759; aceE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycolysis; Isopeptide bond; Magnesium;
KW Oxidoreductase; Pyruvate; Reference proteome; Thiamine pyrophosphate;
KW Ubl conjugation.
FT CHAIN 1..930
FT /note="Pyruvate dehydrogenase E1 component"
FT /id="PRO_0000162246"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 375
FT /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT with Q-Cter in protein Pup)"
FT /evidence="ECO:0000269|PubMed:20066036"
SQ SEQUENCE 930 AA; 103440 MW; 6542FF8373756D53 CRC64;
MTTDFARHDL AQNSNSASEP DRVRVIREGV ASYLPDIDPE ETSEWLESFD TLLQRCGPSR
ARYLMLRLLE RAGEQRVAIP ALTSTDYVNT IPTELEPWFP GDEDVERRYR AWIRWNAAIM
VHRAQRPGVG VGGHISTYAS SAALYEVGFN HFFRGKSHPG GGDQVFIQGH ASPGIYARAF
LEGRLTAEQL DGFRQEHSHV GGGLPSYPHP RLMPDFWEFP TVSMGLGPLN AIYQARFNHY
LHDRGIKDTS DQHVWCFLGD GEMDEPESRG LAHVGALEGL DNLTFVINCN LQRLDGPVRG
NGKIIQELES FFRGAGWNVI KVVWGREWDA LLHADRDGAL VNLMNTTPDG DYQTYKANDG
GYVRDHFFGR DPRTKALVEN MSDQDIWNLK RGGHDYRKVY AAYRAAVDHK GQPTVILAKT
IKGYALGKHF EGRNATHQMK KLTLEDLKEF RDTQRIPVSD AQLEENPYLP PYYHPGLNAP
EIRYMLDRRR ALGGFVPERR TKSKALTLPG RDIYAPLKKG SGHQEVATTM ATVRTFKEVL
RDKQIGPRIV PIIPDEARTF GMDSWFPSLK IYNRNGQLYT AVDADLMLAY KESEVGQILH
EGINEAGSVG SFIAAGTSYA THNEPMIPIY IFYSMFGFQR TGDSFWAAAD QMARGFVLGA
TAGRTTLTGE GLQHADGHSL LLAATNPAVV AYDPAFAYEI AYIVESGLAR MCGENPENIF
FYITVYNEPY VQPPEPENFD PEGVLRGIYR YHAATEQRTN KAQILASGVA MPAALRAAQM
LAAEWDVAAD VWSVTSWGEL NRDGVAIETE KLRHPDRPAG VPYVTRALEN ARGPVIAVSD
WMRAVPEQIR PWVPGTYLTL GTDGFGFSDT RPAARRYFNT DAESQVVAVL EALAGDGEID
PSVPVAAARQ YRIDDVAAAP EQTTDPGPGA
