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B1X8W0 (RHMD_ECODH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
L-rhamnonate dehydratase

Short name=RhamD
EC=4.2.1.90
Gene names
Name:rhmD
Ordered Locus Names:ECDH10B_2407
OrganismEscherichia coli (strain K12 / DH10B) [Complete proteome] [HAMAP]
Taxonomic identifier316385 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length405 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy-L-rhamnonate (KDR) By similarity. HAMAP-Rule MF_01288

Catalytic activity

L-rhamnonate = 2-dehydro-3-deoxy-L-rhamnonate + H2O. HAMAP-Rule MF_01288

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01288

Subunit structure

Homooctamer; tetramer of dimers By similarity. HAMAP-Rule MF_01288

Miscellaneous

Reaction proceeds via a syn dehydration By similarity.

Sequence similarities

Belongs to the mandelate racemase/muconate lactonizing enzyme family. RhamD subfamily.

Ontologies

Keywords
   LigandMagnesium
Metal-binding
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcellular amino acid catabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionL-rhamnonate dehydratase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 405405L-rhamnonate dehydratase HAMAP-Rule MF_01288
PRO_0000351692

Sites

Active site3291Proton acceptor By similarity
Metal binding2261Magnesium By similarity
Metal binding2521Magnesium By similarity
Metal binding2801Magnesium By similarity
Binding site331Substrate By similarity
Binding site591Substrate By similarity
Binding site3491Substrate By similarity
Site3021Increases basicity of active site His By similarity
Site3491Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
B1X8W0 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 747D32E809A7B4DC

FASTA40544,714
        10         20         30         40         50         60 
MENIMTLPKI KQVRAWFTGG ATAEKGAGGG DYHDQGANHW IDDHIATPMS KYRDYEQSRQ 

        70         80         90        100        110        120 
SFGINVLGTL VVEVEAENGQ TGFAVSTAGE MGCFIVEKHL NRFIEGKCVS DIKLIHDQML 

       130        140        150        160        170        180 
SATLYYSGSG GLVMNTISCV DLALWDLFGK VVGLPVYKLL GGAVRDEIQF YATGARPDLA 

       190        200        210        220        230        240 
KEMGFIGGKM PTHWGPHDGD AGIRKDAAMV ADMREKCGED FWLMLDCWMS QDVNYATKLA 

       250        260        270        280        290        300 
HACAPYNLKW IEECLPPQQY ESYRELKRNA PVGMMVTSGE HHGTLQSFRT LSETGIDIMQ 

       310        320        330        340        350        360 
PDVGWCGGLT TLVEIAAIAK SRGQLVVPHG SSVYSHHAVI TFTNTPFSEF LMTSPDCSTM 

       370        380        390        400 
RPQFDPILLN EPVPVNGRIH KSVLDKPGFG VELNRDCNLK RPYSH 

« Hide

References

[1]"The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse."
Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B., Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., Posfai G., Weinstock G.M., Blattner F.R.
J. Bacteriol. 190:2597-2606(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / DH10B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000948 Genomic DNA. Translation: ACB03407.1.
RefSeqYP_001731185.1. NC_010473.1.

3D structure databases

ProteinModelPortalB1X8W0.
SMRB1X8W0. Positions 1-405.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316385.ECDH10B_2407.

Proteomic databases

PRIDEB1X8W0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB03407; ACB03407; ECDH10B_2407.
GeneID6058390.
KEGGecd:ECDH10B_2407.
PATRIC18464683. VBIEscCol59506_2428.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4948.
HOGENOMHOG000113755.
KOK12661.
OMAFCVELEA.
OrthoDBEOG68Q0M0.

Enzyme and pathway databases

BioCycECOL316385:GJ8B-2314-MONOMER.

Family and domain databases

Gene3D3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPMF_01288. Rhamnon_dehydrat.
InterProIPR029065. Enolase_C-like.
IPR029017. Enolase_N_like.
IPR023444. L-Rhamnon_dehydrat.
IPR018110. Mandel_Rmase/mucon_lact_enz_CS.
IPR013342. Mandelate_racemase_C.
IPR013341. Mandelate_racemase_N.
IPR001354. MR_MLE.
[Graphical view]
PANTHERPTHR13794. PTHR13794. 1 hit.
PfamPF01188. MR_MLE. 1 hit.
PF02746. MR_MLE_N. 1 hit.
[Graphical view]
SMARTSM00922. MR_MLE. 1 hit.
[Graphical view]
SUPFAMSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
PROSITEPS00908. MR_MLE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRHMD_ECODH
AccessionPrimary (citable) accession number: B1X8W0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: May 20, 2008
Last modified: June 11, 2014
This is version 43 of the entry and version 1 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