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B5EZH0 (RHMD_SALA4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
L-rhamnonate dehydratase
Short name=RhamD
EC=4.2.1.90
Gene names
Name:rhmD
Ordered Locus Names:SeAg_B2427
OrganismSalmonella agona (strain SL483) [Complete proteome] [HAMAP]
Taxonomic identifier454166 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella ›

Protein attributes

Sequence length401 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.

Subunit structure

Homooctamer; tetramer of dimers By similarity.

Miscellaneous

Reaction proceeds via a syn dehydration By similarity. HAMAP-Rule MF_01288

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: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 401401L-rhamnonate dehydratase HAMAP-Rule MF_01288
PRO_1000165262

Sites

Active site3251Proton acceptor By similarity
Metal binding2221Magnesium By similarity
Metal binding2481Magnesium By similarity
Metal binding2761Magnesium By similarity
Binding site291Substrate By similarity
Binding site551Substrate By similarity
Binding site3451Substrate By similarity
Site2981Increases basicity of active site His By similarity
Site3451Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
B5EZH0 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: 1B66DC07F01C2CA7

FASTA40144,119
        10         20         30         40         50         60 
MTLPKIKHVR AWFIGGATAE KGAGGGDYHD QGGNHWIDDH IATPMSKYRD YEQSRQSFGI 

        70         80         90        100        110        120 
NVLGTLIVEV EAENGQTGFA VSTAGEMGCF IVEKHLNRFI EGKCVSDIKL IHDQMLGATM 

       130        140        150        160        170        180 
YYSGSGGLVM NTISCVDLAL WDLFGKVVGL PVYKLLGGAV RDEIQFYATG ARPDLAKEMG 

       190        200        210        220        230        240 
FIGGKMPTHW GPHDGDAGIR KDAAMVADMR EKCGPDFWLM LDCWMSQDVN YATKLAHACA 

       250        260        270        280        290        300 
PFNLKWIEEC LPPQQYEGYR ELKRNAPAGM MVTSGEHHGT LQSFRTLAET GIDIMQPDVG 

       310        320        330        340        350        360 
WCGGLTTLVE IAALAKSRGQ LVVPHGSSVY SHHAVITFTN TPFSEFLMTS PDCSTLRPQF 

       370        380        390        400 
DPILLDEPVP VNGRIHKSVL DKPGFGVELN RDCHLKRPYS H

« Hide

References

[1]"Complete genome of Salmonella agona strain SL483."
Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M., Leclerc J., Cebula T., Sebastian Y.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SL483.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001138 Genomic DNA. Translation: ACH52764.1.
RefSeqYP_002147247.1. NC_011149.1.

3D structure databases

ProteinModelPortalB5EZH0.
SMRB5EZH0. Positions 1-401.
ModBaseSearch...

Protein-protein interaction databases

STRING454166.SeAg_B2427.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACH52764; ACH52764; SeAg_B2427.
GeneID6796809.
KEGGsea:SeAg_B2427.
PATRIC18483140. VBISalEnt65316_2376.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4948.
HOGENOMHOG000113755.
KOK12661.
OMATGEHEYS.
ProtClustDBPRK15440.

Enzyme and pathway databases

BioCycSENT454166:GHBA-4453-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.
PTHR13794:SF27. PTHR13794:SF27. 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.
PS00909. MR_MLE_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRHMD_SALA4
AccessionPrimary (citable) accession number: B5EZH0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: October 14, 2008
Last modified: May 1, 2013
This is version 29 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

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