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A0R0B0

- ODP1_MYCS2

UniProt

A0R0B0 - ODP1_MYCS2

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Protein

Pyruvate dehydrogenase E1 component

Gene

aceE

Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

Catalytic activityi

Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.

Cofactori

Protein has several cofactor binding sites:

GO - Molecular functioni

  1. pyruvate dehydrogenase (acetyl-transferring) activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

Magnesium, Pyruvate, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciMSME246196:GJ4Y-4322-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyruvate dehydrogenase E1 component (EC:1.2.4.1)
Short name:
PDH E1 component
Gene namesi
Name:aceE
Ordered Locus Names:MSMEG_4323, MSMEI_4223
OrganismiMycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Taxonomic identifieri246196 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium
ProteomesiUP000000757: Chromosome, UP000006158: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 929929Pyruvate dehydrogenase E1 componentPRO_0000396809Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki375 – 375Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Interactioni

Subunit structurei

Homodimer. Part of the PDH complex, consisting of multiple copies of AceE (E1), DlaT (E2) and Lpd (E3).By similarity

Protein-protein interaction databases

STRINGi246196.MSMEG_4323.

Structurei

3D structure databases

ProteinModelPortaliA0R0B0.
SMRiA0R0B0. Positions 85-916.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiCOG2609.
HOGENOMiHOG000115215.
KOiK00163.
OMAiLVHLMNT.
OrthoDBiEOG6BW4TW.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR004660. 2-oxoA_DH_E1.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005474. Transketolase_N.
[Graphical view]
PfamiPF00456. Transketolase_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAMiSSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsiTIGR00759. aceE. 1 hit.

Sequencei

Sequence statusi: Complete.

A0R0B0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTTEFVRQDL AQNSSTAAEP DRVRVIREGV ASYLPDIDTE ETAEWLESFD
60 70 80 90 100
ELLERSGPAR ARYLMLRLLE RAGEQRVAIP ALTSTDYVNT IPTELEPWFP
110 120 130 140 150
GDEDVERRYR AWIRWNAAIM VHRAQRPGVG VGGHISTYAS SATLYEVGFN
160 170 180 190 200
HFFRGKSHPG GGDHVFIQGH ASPGIYARAF LEGRLTTDQL DGFRQEHSHS
210 220 230 240 250
GGGLPSYPHP RLMPDFWEFP TVSMGLGPMN AIYQARFNHY LHDRGIKDTS
260 270 280 290 300
DQHVWAFLGD GEMDEPESRG LIQVAANEAL DNLTFVINCN LQRLDGPVRG
310 320 330 340 350
NGKIIQELES FFRGAGWNVI KVVWGREWDV LLHADRDGAL VNLMNSTPDG
360 370 380 390 400
DYQTYKANDG AYVRDHFFGR DPRTKALVAD MSDQEIWNLK RGGHDYRKVY
410 420 430 440 450
AAYRAAMEHK GQPTVILAKT IKGYTLGQHF EGRNATHQMK KLALEDLKNF
460 470 480 490 500
RDVTRVPVSD AQLEEDPYLP PYYHPGPEAP EIRYLLERRR ALGGFVPSRR
510 520 530 540 550
TKSKPLALPG SDTYKALKKG SGSQAVATTM ATVRTFKELL RDKNIGPRIV
560 570 580 590 600
PIIPDEARTF GMDSWFPSLK IYNRNGQLYT SVDSELMLAY KESEVGQILH
610 620 630 640 650
EGINEAGSTS SFTAVGTSYS THDEPMIPIY IFYSMFGFQR TGDGLWAAAD
660 670 680 690 700
QMARGFVLGA TAGRTTLTGE GLQHADGHSL LLASTNPAAV TYDPAFAYEI
710 720 730 740 750
AHIIESGLQR MYGEDPENVF FYLTIYNEPY QQPAEPENLD VEALLKGLYL
760 770 780 790 800
YRPAPEKRAK SAQILASGVA MPEALRAADL LASDWDVAAD VWSVTSWGEL
810 820 830 840 850
NREGVAIEKH RLRHPDEPAG TPHVTSALAD AAGPVIAVSD WMRAVPEQIR
860 870 880 890 900
PWVPGTYVTL GTDGFGFSDT RPAARRYFNT DAESVVVAVL QGLARDGEID
910 920
ASVAAQAAEQ YRIDDVSAAG VSYADTGSA
Length:929
Mass (Da):103,077
Last modified:January 9, 2007 - v1
Checksum:i5CB137A1D69BFB23
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK72760.1.
CP001663 Genomic DNA. Translation: AFP40679.1.
RefSeqiYP_006568974.1. NC_018289.1.
YP_888598.1. NC_008596.1.

Genome annotation databases

EnsemblBacteriaiABK72760; ABK72760; MSMEG_4323.
AFP40679; AFP40679; MSMEI_4223.
GeneIDi4531364.
KEGGimsm:MSMEG_4323.
PATRICi18081001. VBIMycSme59918_4241.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA. Translation: ABK72760.1 .
CP001663 Genomic DNA. Translation: AFP40679.1 .
RefSeqi YP_006568974.1. NC_018289.1.
YP_888598.1. NC_008596.1.

3D structure databases

ProteinModelPortali A0R0B0.
SMRi A0R0B0. Positions 85-916.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 246196.MSMEG_4323.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ABK72760 ; ABK72760 ; MSMEG_4323 .
AFP40679 ; AFP40679 ; MSMEI_4223 .
GeneIDi 4531364.
KEGGi msm:MSMEG_4323.
PATRICi 18081001. VBIMycSme59918_4241.

Phylogenomic databases

eggNOGi COG2609.
HOGENOMi HOG000115215.
KOi K00163.
OMAi LVHLMNT.
OrthoDBi EOG6BW4TW.

Enzyme and pathway databases

BioCyci MSME246196:GJ4Y-4322-MONOMER.

Family and domain databases

Gene3Di 3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProi IPR004660. 2-oxoA_DH_E1.
IPR029061. THDP-binding.
IPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR005474. Transketolase_N.
[Graphical view ]
Pfami PF00456. Transketolase_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000156. Pyruvate_dh_E1. 1 hit.
SUPFAMi SSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsi TIGR00759. aceE. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
    Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  2. "Interrupted coding sequences in Mycobacterium smegmatis: authentic mutations or sequencing errors?"
    Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C., Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.
    Genome Biol. 8:R20.1-R20.9(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  3. "Ortho-proteogenomics: multiple proteomes investigation through orthology and a new MS-based protocol."
    Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M., Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.
    Genome Res. 19:128-135(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700084 / mc(2)155.
  4. Cited for: PUPYLATION AT LYS-375, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiODP1_MYCS2
AccessioniPrimary (citable) accession number: A0R0B0
Secondary accession number(s): I7GD92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: January 9, 2007
Last modified: November 26, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

External Data

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