Q10504 (ODP1_MYCTU) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pyruvate dehydrogenase E1 component
Short name=PDH E1 component
EC=1.2.4.1

Gene names

Name:	aceE
Ordered Locus Names:	Rv2241, MT2301
ORF Names:	MTCY427.22

Organism

Mycobacterium tuberculosis [Reference proteome] [HAMAP]

Taxonomic identifier

1773 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex

Protein attributes

Sequence length	901 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. AceE has reductase activity with pyruvate but does not react with 2-oxoglutarate. Ref.3
Catalytic activity	Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
Cofactor	Magnesium. Ref.3 Thiamine pyrophosphate. Ref.3
Subunit structure	Homodimer By similarity. Makes part of the PDH complex, consisting of multiple copies of AceE (E1), DlaT (E2) and Lpd (E3). Ref.3
Biophysicochemical properties	Kinetic parameters: KM=47 µM for pyruvate Ref.3 pH dependence: Optimum pH is 8.0 for PDH complex activity. Half-maximal activity is observed at pH 7.0 and pH 9.0. Activity is abolished at pH < 5.

Ontologies

Keywords
Biological process	Glycolysis
Ligand	Magnesium Pyruvate Thiamine pyrophosphate
Molecular function	Oxidoreductase
PTM	Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glycolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cell wall Inferred from direct assay PubMed 20825248. Source: MTBBASE extracellular region Inferred from direct assay PubMed 17443846. Source: MTBBASE plasma membrane Inferred from direct assay PubMed 14532352PubMed 15525680. Source: MTBBASE pyruvate dehydrogenase complex Inferred from direct assay Ref.3. Source: MTBBASE
Molecular_function	magnesium ion binding Inferred from direct assay Ref.3. Source: MTBBASE pyruvate dehydrogenase (acetyl-transferring) activity Inferred from direct assay Ref.3. Source: MTBBASE
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 901	901	Pyruvate dehydrogenase E1 component		PRO_0000162246
Amino acid modifications
	Cross-link	346		Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

Sequences

	Sequence		Length	Mass (Da)
	Q10504 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: F7910AA5722539BF	FASTA	901	100,217
	10 20 30 40 50 60 MASYLPDIDP EETSEWLESF DTLLQRCGPS RARYLMLRLL ERAGEQRVAI PALTSTDYVN 70 80 90 100 110 120 TIPTELEPWF PGDEDVERRY RAWIRWNAAI MVHRAQRPGV GVGGHISTYA SSAALYEVGF 130 140 150 160 170 180 NHFFRGKSHP GGGDQVFIQG HASPGIYARA FLEGRLTAEQ LDGFRQEHSH VGGGLPSYPH 190 200 210 220 230 240 PRLMPDFWEF PTVSMGLGPL NAIYQARFNH YLHDRGIKDT SDQHVWCFLG DGEMDEPESR 250 260 270 280 290 300 GLAHVGALEG LDNLTFVINC NLQRLDGPVR GNGKIIQELE SFFRGAGWNV IKVVWGREWD 310 320 330 340 350 360 ALLHADRDGA LVNLMNTTPD GDYQTYKAND GGYVRDHFFG RDPRTKALVE NMSDQDIWNL 370 380 390 400 410 420 KRGGHDYRKV YAAYRAAVDH KGQPTVILAK TIKGYALGKH FEGRNATHQM KKLTLEDLKE 430 440 450 460 470 480 FRDTQRIPVS DAQLEENPYL PPYYHPGLNA PEIRYMLDRR RALGGFVPER RTKSKALTLP 490 500 510 520 530 540 GRDIYAPLKK GSGHQEVATT MATVRTFKEV LRDKQIGPRI VPIIPDEART FGMDSWFPSL 550 560 570 580 590 600 KIYNRNGQLY TAVDADLMLA YKESEVGQIL HEGINEAGSV GSFIAAGTSY ATHNEPMIPI 610 620 630 640 650 660 YIFYSMFGFQ RTGDSFWAAA DQMARGFVLG ATAGRTTLTG EGLQHADGHS LLLAATNPAV 670 680 690 700 710 720 VAYDPAFAYE IAYIVESGLA RMCGENPENI FFYITVYNEP YVQPPEPENF DPEGVLRGIY 730 740 750 760 770 780 RYHAATEQRT NKAQILASGV AMPAALRAAQ MLAAEWDVAA DVWSVTSWGE LNRDGVAIET 790 800 810 820 830 840 EKLRHPDRPA GVPYVTRALE NARGPVIAVS DWMRAVPEQI RPWVPGTYLT LGTDGFGFSD 850 860 870 880 890 900 TRPAARRYFN TDAESQVVAV LEALAGDGEI DPSVPVAAAR QYRIDDVAAA PEQTTDPGPG A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence." Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K. , Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S., Barrell B.G. Nature 393:537-544(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25618 / H37Rv.
[2]	"Whole-genome comparison of Mycobacterium tuberculosis clinical and laboratory strains." Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K., Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., Delcher A., Utterback T.R. , Weidman J.F., Khouri H.M., Gill J., Mikula A., Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M. J. Bacteriol. 184:5479-5490(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CDC 1551 / Oshkosh.
[3]	"Mycobacterium tuberculosis appears to lack alpha-ketoglutarate dehydrogenase and encodes pyruvate dehydrogenase in widely separated genes." Tian J., Bryk R., Shi S., Erdjument-Bromage H., Tempst P., Nathan C. Mol. Microbiol. 57:859-868(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, IDENTIFICATION IN THE PDH COMPLEX. Strain: ATCC 25618 / H37Rv.
[4]	"Prokayrotic ubiquitin-like protein (Pup) proteome of Mycobacterium tuberculosis." Festa R.A., McAllister F., Pearce M.J., Mintseris J., Burns K.E., Gygi S.P., Darwin K.H. PLoS ONE 5:E8589-E8589(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PUPYLATION AT LYS-346, IDENTIFICATION BY MASS SPECTROMETRY. Strain: ATCC 25618 / H37Rv.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000516 Genomic DNA. Translation: AAK46585.1. AL123456 Genomic DNA. Translation: CCP45021.1.
PIR	E70778.
RefSeq	NP_216757.3. NC_000962.3. NP_336771.1. NC_002755.2. YP_006515664.1. NC_018143.1.
3D structure databases
ProteinModelPortal	Q10504.
SMR	Q10504. Positions 56-885.
ModBase	Search...
Protein-protein interaction databases
STRING	83332.Rv2241.
Proteomic databases
PaxDb	Q10504.
PRIDE	Q10504.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAK46585; AAK46585; MT2301.
GeneID	13318934. 887246. 924124.
KEGG	mtc:MT2301. mtu:Rv2241.
PATRIC	18126809. VBIMycTub22151_2515.
Organism-specific databases
TubercuList	Rv2241.
Phylogenomic databases
eggNOG	COG2609.
HOGENOM	HOG000115215.
KO	K00163.
OMA	PEETGEW.
ProtClustDB	PRK09405.
Family and domain databases
Gene3D	3.40.50.920. 1 hit.
InterPro	IPR004660. 2-oxoA_DH_E1. IPR009014. Transketo_C/Pyr-ferredox_oxred. IPR015941. Transketolase-like_C. IPR005474. Transketolase_N. [Graphical view]
Pfam	PF00456. Transketolase_N. 1 hit. [Graphical view]
PIRSF	PIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAM	SSF52922. Transketo_C_like. 1 hit.
TIGRFAMs	TIGR00759. aceE. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ODP1_MYCTU

Accession

Primary (citable) accession number: Q10504
Secondary accession number(s): L0TBX6

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 29, 2013
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program