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Protein

N-acetylmuramic acid 6-phosphate etherase

Gene

murQ

Organism
Salmonella gallinarum (strain 287/91 / NCTC 13346)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.UniRule annotation

Catalytic activityi

(R)-lactate + N-acetyl-D-glucosamine 6-phosphate = N-acetylmuramate 6-phosphate + H2O.UniRule annotation

Pathwayi: 1,6-anhydro-N-acetylmuramate degradation

This protein is involved in the pathway 1,6-anhydro-N-acetylmuramate degradation, which is part of Amino-sugar metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway 1,6-anhydro-N-acetylmuramate degradation and in Amino-sugar metabolism.

Pathwayi: N-acetylmuramate degradation

This protein is involved in the pathway N-acetylmuramate degradation, which is part of Amino-sugar metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway N-acetylmuramate degradation and in Amino-sugar metabolism.

Pathwayi: peptidoglycan recycling

This protein is involved in the pathway peptidoglycan recycling, which is part of Cell wall biogenesis.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway peptidoglycan recycling and in Cell wall biogenesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei83 – 831Proton donorUniRule annotation
Active sitei114 – 1141UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciSENT550538:GJ93-2555-MONOMER.
UniPathwayiUPA00342.
UPA00343.
UPA00544.

Names & Taxonomyi

Protein namesi
Recommended name:
N-acetylmuramic acid 6-phosphate etheraseUniRule annotation (EC:4.2.1.126UniRule annotation)
Short name:
MurNAc-6-P etheraseUniRule annotation
Alternative name(s):
N-acetylmuramic acid 6-phosphate hydrolaseUniRule annotation
N-acetylmuramic acid 6-phosphate lyaseUniRule annotation
Gene namesi
Name:murQUniRule annotation
Ordered Locus Names:SG2608
OrganismiSalmonella gallinarum (strain 287/91 / NCTC 13346)
Taxonomic identifieri550538 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000008321 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 297297N-acetylmuramic acid 6-phosphate etherasePRO_1000092314Add
BLAST

Expressioni

Inductioni

Induced by MurNAc 6-phosphate that releases the repressor MurR from the DNA. Repressed by MurR in the absence of MurNAc 6-phosphate.UniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB5RD39.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini55 – 218164SISUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the GCKR-like family. MurNAc-6-P etherase subfamily.UniRule annotation
Contains 1 SIS domain.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000084045.
KOiK07106.
OMAiAIRIVMQ.
OrthoDBiPOG091H05F1.

Family and domain databases

HAMAPiMF_00068. MurQ. 1 hit.
InterProiIPR005488. Etherase_MurQ.
IPR005486. Glucokinase_regulatory_CS.
IPR001347. SIS.
[Graphical view]
PfamiPF01380. SIS. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00274. TIGR00274. 1 hit.
PROSITEiPS01272. GCKR. 1 hit.
PS51464. SIS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B5RD39-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLGTLVSET RNPQTMDLDA LPTPELVKRF NEQDTRVAEA VKATLPDVAR
60 70 80 90 100
AVDAAVAALK SGGRIIYMGA GTSGRLGVLD ASECPPTFGV PHGLVVGLIA
110 120 130 140 150
GGPGALLKAV EGAEDSQQAG EDDLVALNLQ EQDLVVGLAA SGRTPYVIGG
160 170 180 190 200
LRYARQSGCT TVAVSCNPDS PIAREANIAI SPVVGPEALT GSTRLKSGTA
210 220 230 240 250
QKMVLNMIST GAMVKFGKVY QNLMVDMKAT NVKLVDRACR MVVEATGIGR
260 270 280 290
EEAETLLKQT DFEVKPAILM ALTGLDAAAA REKLAAHQGF LRAALEH
Length:297
Mass (Da):30,976
Last modified:November 4, 2008 - v1
Checksum:i9A04C440A821477C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM933173 Genomic DNA. Translation: CAR38425.1.
RefSeqiWP_001048537.1. NC_011274.1.

Genome annotation databases

EnsemblBacteriaiCAR38425; CAR38425; EBG00000232418.
KEGGiseg:SG2608.
PATRICi18503697. VBISalEnt1629_2760.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM933173 Genomic DNA. Translation: CAR38425.1.
RefSeqiWP_001048537.1. NC_011274.1.

3D structure databases

ProteinModelPortaliB5RD39.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAR38425; CAR38425; EBG00000232418.
KEGGiseg:SG2608.
PATRICi18503697. VBISalEnt1629_2760.

Phylogenomic databases

HOGENOMiHOG000084045.
KOiK07106.
OMAiAIRIVMQ.
OrthoDBiPOG091H05F1.

Enzyme and pathway databases

UniPathwayiUPA00342.
UPA00343.
UPA00544.
BioCyciSENT550538:GJ93-2555-MONOMER.

Family and domain databases

HAMAPiMF_00068. MurQ. 1 hit.
InterProiIPR005488. Etherase_MurQ.
IPR005486. Glucokinase_regulatory_CS.
IPR001347. SIS.
[Graphical view]
PfamiPF01380. SIS. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00274. TIGR00274. 1 hit.
PROSITEiPS01272. GCKR. 1 hit.
PS51464. SIS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMURQ_SALG2
AccessioniPrimary (citable) accession number: B5RD39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 4, 2008
Last modified: September 7, 2016
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

A lyase-type mechanism (elimination/hydration) is suggested for the cleavage of the lactyl ether bond of MurNAc 6-phosphate, with the formation of an alpha,beta-unsaturated aldehyde intermediate with (E)-stereochemistry, followed by the syn addition of water to give product.UniRule annotation

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.