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P77243 (PRPD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
2-methylcitrate dehydratase

EC=4.2.1.79
Gene names
Name:prpD
Synonyms:yahT
Ordered Locus Names:b0334, JW0325
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length483 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the dehydration of 2-methylcitrate to 2-methyl-cis-aconitate. Also seems to be responsible for the residual aconitase activity of the acnAB-null strain.

Catalytic activity

(2S,3S)-2-hydroxybutane-1,2,3-tricarboxylate = (Z)-but-2-ene-1,2,3-tricarboxylate + H2O. Ref.5

Cofactor

Binds 1 2Fe-2S cluster.

Pathway

Organic acid metabolism; propanoate degradation.

Subunit structure

Monomer.

Sequence similarities

Belongs to the PrpD family.

Biophysicochemical properties

Kinetic parameters:

KM=0.44 mM for (2S,3S)-2-methylcitrate Ref.5

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 4834822-methylcitrate dehydratase
PRO_0000215023

Secondary structure

............................................................................ 483
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P77243 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 965252C8983E6F64

FASTA48353,952
        10         20         30         40         50         60 
MSAQINNIRP EFDREIVDIV DYVMNYEISS KVAYDTAHYC LLDTLGCGLE ALEYPACKKL 

        70         80         90        100        110        120 
LGPIVPGTVV PNGVRVPGTQ FQLDPVQAAF NIGAMIRWLD FNDTWLAAEW GHPSDNLGGI 

       130        140        150        160        170        180 
LATADWLSRN AVASGKAPLT MKQVLTAMIK AHEIQGCIAL ENSFNRVGLD HVLLVKVAST 

       190        200        210        220        230        240 
AVVAEMLGLT REEILNAVSL AWVDGQSLRT YRHAPNTGTR KSWAAGDATS RAVRLALMAK 

       250        260        270        280        290        300 
TGEMGYPSAL TAPVWGFYDV SFKGESFRFQ RPYGSYVMEN VLFKISFPAE FHSQTAVEAA 

       310        320        330        340        350        360 
MTLYEQMQAA GKTAADIEKV TIRTHEACIR IIDKKGPLNN PADRDHCIQY MVAIPLLFGR 

       370        380        390        400        410        420 
LTAADYEDNV AQDKRIDALR EKINCFEDPA FTADYHDPEK RAIANAITLE FTDGTRFEEV 

       430        440        450        460        470        480 
VVEYPIGHAR RRQDGIPKLV DKFKINLARQ FPTRQQQRIL EVSLDRARLE QMPVNEYLDL 


YVI 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"AcnC of Escherichia coli is a 2-methylcitrate dehydratase (PrpD) that can use citrate and isocitrate as substrates."
Blank L., Green J., Guest J.R.
Microbiology 148:133-146(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-13, CHARACTERIZATION.
[5]"Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase."
Brock M., Maerker C., Schuetz A., Voelker U., Buckel W.
Eur. J. Biochem. 269:6184-6194(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
[6]"Crystal structure of 2-methylcitrate dehydratase."
New York structural genomix research consortium (NYSGXRC)
Submitted (FEB-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U73857 Genomic DNA. Translation: AAB18058.1.
U00096 Genomic DNA. Translation: AAC73437.1.
AP009048 Genomic DNA. Translation: BAE76116.1.
PIRF64760.
RefSeqNP_414868.1. NC_000913.3.
YP_488628.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SZQX-ray2.70A/B1-483[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10580N.
IntActP77243. 4 interactions.
MINTMINT-1309441.
STRING511145.b0334.

Proteomic databases

PRIDEP77243.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73437; AAC73437; b0334.
BAE76116; BAE76116; BAE76116.
GeneID12930816.
945931.
KEGGecj:Y75_p0323.
eco:b0334.
PATRIC32115799. VBIEscCol129921_0341.

Organism-specific databases

EchoBASEEB3371.
EcoGeneEG13603. prpD.

Phylogenomic databases

eggNOGCOG2079.
HOGENOMHOG000159916.
KOK01720.
OMATAPQWGF.
OrthoDBEOG6RC3K5.
PhylomeDBP77243.

Enzyme and pathway databases

BioCycEcoCyc:G6199-MONOMER.
ECOL316407:JW0325-MONOMER.
MetaCyc:G6199-MONOMER.
BRENDA4.2.1.79. 2026.
SABIO-RKP77243.
UniPathwayUPA00946.

Gene expression databases

GenevestigatorP77243.

Family and domain databases

InterProIPR012705. 2Me_IsoCit_deHydtase_PrpD.
IPR005656. MmgE_PrpD.
[Graphical view]
PANTHERPTHR16943. PTHR16943. 1 hit.
PfamPF03972. MmgE_PrpD. 1 hit.
[Graphical view]
SUPFAMSSF103378. SSF103378. 1 hit.
TIGRFAMsTIGR02330. prpD. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP77243.
PROP77243.

Entry information

Entry namePRPD_ECOLI
AccessionPrimary (citable) accession number: P77243
Secondary accession number(s): Q2MC90
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene