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A6TBU8 (RHMD_KLEP7) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 42. 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:KPN78578_26080
ORF Names:KPN_02652
OrganismKlebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578) [Complete proteome] [HAMAP]
Taxonomic identifier272620 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeKlebsiella

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. 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 – 401401L-rhamnonate dehydratase HAMAP-Rule MF_01288
PRO_0000351700

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
A6TBU8 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: AFB4385C9AF18AB7

FASTA40144,202
        10         20         30         40         50         60 
MTLPKIKHVR AWFIGGATAE QGAGGGDYHD QGANHWIDDH IATPMSKYKQ YEQSRQSFGI 

        70         80         90        100        110        120 
NVLGTLIVEV EADNGQTGFA VSTAGEMGCF IVEKHLNRFI EGKCVSDIKL IHDQMLNATL 

       130        140        150        160        170        180 
YYAGSGGLVM NTISCVDLAL WDLFGKVVGL PVYKLLGGAV RDEIQFYATG ARPDLAQEMG 

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

       250        260        270        280        290        300 
PYNLKWIEEC LPPQQYEGYR ELKRQAPAGM MVTSGEHHGT LQSFRTLSET GIDIMQPDVG 

       310        320        330        340        350        360 
WCGGLTTLVE IAAIAKARGQ LVVPHGSSVY SHHAVITFTN TPFSEFLMTS PDCATLRPQF 

       370        380        390        400 
DPILLGEPVP ERGRIHKSVL DKPGFGVELN RDCNLKRPYQ H 

« Hide

References

[1]The Klebsiella pneumonia Genome Sequencing Project
McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P., Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700721 / MGH 78578.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000647 Genomic DNA. Translation: ABR78069.1.
RefSeqYP_001336299.1. NC_009648.1.

3D structure databases

ProteinModelPortalA6TBU8.
SMRA6TBU8. Positions 1-401.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272620.KPN_02652.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR78069; ABR78069; KPN_02652.
GeneID5341828.
KEGGkpn:KPN_02652.
PATRIC20459598. VBIKlePne13394_2673.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4948.
HOGENOMHOG000113755.
KOK12661.
OMAINWWEEC.
OrthoDBEOG68Q0M0.
ProtClustDBPRK15440.

Enzyme and pathway databases

BioCycKPNE272620:GKDC-2652-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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRHMD_KLEP7
AccessionPrimary (citable) accession number: A6TBU8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: August 21, 2007
Last modified: February 19, 2014
This is version 42 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