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Protein

L-rhamnonate dehydratase

Gene

rhmD

Organism
Escherichia coli (strain K12 / DH10B)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the dehydration of L-rhamnonate to 2-keto-3-deoxy-L-rhamnonate (KDR).UniRule annotation

Catalytic activityi

L-rhamnonate = 2-dehydro-3-deoxy-L-rhamnonate + H2O.UniRule annotation

Cofactori

Mg2+UniRule annotationNote: Binds 1 Mg2+ ion per subunit.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei33SubstrateUniRule annotation1
Binding sitei59SubstrateUniRule annotation1
Metal bindingi226MagnesiumUniRule annotation1
Metal bindingi252MagnesiumUniRule annotation1
Metal bindingi280MagnesiumUniRule annotation1
Sitei302Increases basicity of active site HisUniRule annotation1
Active sitei329Proton acceptorUniRule annotation1
Binding sitei349SubstrateUniRule annotation1
Sitei349Transition state stabilizerUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
L-rhamnonate dehydrataseUniRule annotation (EC:4.2.1.90UniRule annotation)
Short name:
RhamDUniRule annotation
Gene namesi
Name:rhmDUniRule annotation
Ordered Locus Names:ECDH10B_2407
OrganismiEscherichia coli (strain K12 / DH10B)
Taxonomic identifieri316385 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003516921 – 405L-rhamnonate dehydrataseAdd BLAST405

Interactioni

Subunit structurei

Homooctamer; tetramer of dimers.UniRule annotation

Protein-protein interaction databases

STRINGi316385.ECDH10B_2407.

Structurei

3D structure databases

ProteinModelPortaliB1X8W0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105CXK. Bacteria.
COG4948. LUCA.
HOGENOMiHOG000113755.
KOiK12661.
OMAiINWWEEC.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_01288. Rhamnon_dehydrat. 1 hit.
InterProiIPR029065. 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_dom.
IPR001354. MR/MLE/MAL.
[Graphical view]
PANTHERiPTHR13794. PTHR13794. 1 hit.
PfamiPF13378. MR_MLE_C. 1 hit.
PF02746. MR_MLE_N. 1 hit.
[Graphical view]
SMARTiSM00922. MR_MLE. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
PROSITEiPS00908. MR_MLE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B1X8W0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MENIMTLPKI KQVRAWFTGG ATAEKGAGGG DYHDQGANHW IDDHIATPMS
60 70 80 90 100
KYRDYEQSRQ SFGINVLGTL VVEVEAENGQ TGFAVSTAGE MGCFIVEKHL
110 120 130 140 150
NRFIEGKCVS DIKLIHDQML SATLYYSGSG GLVMNTISCV DLALWDLFGK
160 170 180 190 200
VVGLPVYKLL GGAVRDEIQF YATGARPDLA KEMGFIGGKM PTHWGPHDGD
210 220 230 240 250
AGIRKDAAMV ADMREKCGED FWLMLDCWMS QDVNYATKLA HACAPYNLKW
260 270 280 290 300
IEECLPPQQY ESYRELKRNA PVGMMVTSGE HHGTLQSFRT LSETGIDIMQ
310 320 330 340 350
PDVGWCGGLT TLVEIAAIAK SRGQLVVPHG SSVYSHHAVI TFTNTPFSEF
360 370 380 390 400
LMTSPDCSTM RPQFDPILLN EPVPVNGRIH KSVLDKPGFG VELNRDCNLK

RPYSH
Length:405
Mass (Da):44,714
Last modified:May 20, 2008 - v1
Checksum:i747D32E809A7B4DC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000948 Genomic DNA. Translation: ACB03407.1.

Genome annotation databases

EnsemblBacteriaiACB03407; ACB03407; ECDH10B_2407.
KEGGiecd:ECDH10B_2407.
PATRICi18464683. VBIEscCol59506_2428.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000948 Genomic DNA. Translation: ACB03407.1.

3D structure databases

ProteinModelPortaliB1X8W0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi316385.ECDH10B_2407.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACB03407; ACB03407; ECDH10B_2407.
KEGGiecd:ECDH10B_2407.
PATRICi18464683. VBIEscCol59506_2428.

Phylogenomic databases

eggNOGiENOG4105CXK. Bacteria.
COG4948. LUCA.
HOGENOMiHOG000113755.
KOiK12661.
OMAiINWWEEC.

Family and domain databases

Gene3Di3.20.20.120. 1 hit.
3.30.390.10. 1 hit.
HAMAPiMF_01288. Rhamnon_dehydrat. 1 hit.
InterProiIPR029065. 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_dom.
IPR001354. MR/MLE/MAL.
[Graphical view]
PANTHERiPTHR13794. PTHR13794. 1 hit.
PfamiPF13378. MR_MLE_C. 1 hit.
PF02746. MR_MLE_N. 1 hit.
[Graphical view]
SMARTiSM00922. MR_MLE. 1 hit.
[Graphical view]
SUPFAMiSSF51604. SSF51604. 1 hit.
SSF54826. SSF54826. 1 hit.
PROSITEiPS00908. MR_MLE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRHMD_ECODH
AccessioniPrimary (citable) accession number: B1X8W0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 14, 2008
Last sequence update: May 20, 2008
Last modified: November 2, 2016
This is version 57 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Reaction proceeds via a syn dehydration.UniRule annotation

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.