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A9BQY2 (RHMD_DELAS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 34. 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:Daci_0291
OrganismDelftia acidovorans (strain DSM 14801 / SPH-1) [Complete proteome] [HAMAP]
Taxonomic identifier398578 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeDelftia

Protein attributes

Sequence length395 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.

Sequence caution

The sequence ABX32937.1 differs from that shown. Reason: Erroneous initiation.

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 – 395395L-rhamnonate dehydratase HAMAP-Rule MF_01288
PRO_0000351690

Sites

Active site3191Proton acceptor By similarity
Metal binding2151Magnesium By similarity
Metal binding2411Magnesium By similarity
Metal binding2691Magnesium By similarity
Binding site231Substrate By similarity
Binding site491Substrate By similarity
Binding site3391Substrate By similarity
Site2921Increases basicity of active site His By similarity
Site3391Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A9BQY2 [UniParc].

Last modified October 14, 2008. Version 2.
Checksum: 96CD5CB9833E4E1F

FASTA39543,944
        10         20         30         40         50         60 
MTQIPTIKQV RAFTLKGGGA DYHDQSDGHW IDDHIATPMA KYPEYRQSRR SFGINVLGTL 

        70         80         90        100        110        120 
VVEIEDSAGR VGFAVTTGGE PAAYIVEKHL ARFLEGARVT DIERIWDQMY LSTLYYGRKG 

       130        140        150        160        170        180 
IVINTISGVD LALWDLLGKV RGEPVHQLLG GAVRDELQFY ATGARPDLAQ KMGFIGGKMP 

       190        200        210        220        230        240 
LHHGPAEGEE GLRRNLQELA TMRERVGPDF WLMLDCWMSL DVNYATRLAQ GAQAHGLKWI 

       250        260        270        280        290        300 
EEALPPDDYW GYAALRKNVP TGMLVTTGEH EATRWGFRQL LEMGCCDIIQ PDVGWCGGIT 

       310        320        330        340        350        360 
ELLKISALAD AHQALVIPHG SSVYSYHFVA TRHNSPFAEF LMMAPKADEV VPMFHPQLLG 

       370        380        390 
EPVPVNGRMR LSALDRPGFG VELNPECALH RPYTH 

« Hide

References

[1]"Complete sequence of Delftia acidovorans DSM 14801 / SPH-1."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.
Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 14801 / SPH-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000884 Genomic DNA. Translation: ABX32937.1. Different initiation.
RefSeqYP_001561322.1. NC_010002.1.

3D structure databases

ProteinModelPortalA9BQY2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING398578.Daci_0291.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX32937; ABX32937; Daci_0291.
GeneID5745827.
KEGGdac:Daci_0291.
PATRIC21634395. VBIDelAci41351_0303.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4948.
HOGENOMHOG000113755.
KOK12661.
OrthoDBEOG68Q0M0.
ProtClustDBPRK15440.

Enzyme and pathway databases

BioCycDACI398578:GHK3-291-MONOMER.

Family and domain databases

HAMAPMF_01288. Rhamnon_dehydrat.
InterProIPR023444. 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]
PROSITEPS00908. MR_MLE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRHMD_DELAS
AccessionPrimary (citable) accession number: A9BQY2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: October 14, 2008
Last modified: February 19, 2014
This is version 34 of the entry and version 2 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