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Protein

N-acetylmuramic acid 6-phosphate etherase

Gene

murQ

Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
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.UniRule annotation

Catalytic activityi

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

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei94Proton donorUniRule annotation1
Active sitei125UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

UniPathwayiUPA00342.

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:SAV_3924
OrganismiStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Taxonomic identifieri227882 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces
Proteomesi
  • UP000000428 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002496661 – 311N-acetylmuramic acid 6-phosphate etheraseAdd BLAST311

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi227882.SAV_3924.

Structurei

3D structure databases

ProteinModelPortaliQ82GH3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini66 – 229SISUniRule annotationAdd BLAST164

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105E15. Bacteria.
COG2103. LUCA.
HOGENOMiHOG000084045.
KOiK07106.
OMAiAIRIVMQ.
OrthoDBiPOG091H05F1.

Family and domain databases

CDDicd05007. SIS_Etherase. 1 hit.
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.

Q82GH3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSMSHHRSL QAELETLTTE AFRPELAEID QLPTLEIARL MNGEDATVPA
60 70 80 90 100
AVAARLPQIA AAIDAVADRM ARGGRLVYAG AGTAGRLGVL DASECPPTFN
110 120 130 140 150
TDPSEVVGLI AGGPSAMVTS IEGAEDSKEL AAGDLAGLGL TADDTVVGVS
160 170 180 190 200
ASGRTPYAIG AVEYARARGA LTVGLSCNAD SALAAAADHG IEIVAGPELL
210 220 230 240 250
TGSTRLKAGT AQKLVLNMLS TITMIRLGKT YGNLMVDVRA SNEKLRARSR
260 270 280 290 300
RIVALATGAA DEEVERALAA TDGEVKNAIL TILGGVDGPT AARLLEESDG
310
HLRAALAAAP R
Length:311
Mass (Da):31,786
Last modified:June 1, 2003 - v1
Checksum:i464299CD09BEC706
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000030 Genomic DNA. Translation: BAC71636.1.
RefSeqiWP_010985355.1. NZ_JZJK01000090.1.

Genome annotation databases

EnsemblBacteriaiBAC71636; BAC71636; SAVERM_3924.
KEGGisma:SAV_3924.
PATRICi23721567. VBIStrAve112782_4186.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000030 Genomic DNA. Translation: BAC71636.1.
RefSeqiWP_010985355.1. NZ_JZJK01000090.1.

3D structure databases

ProteinModelPortaliQ82GH3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi227882.SAV_3924.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAC71636; BAC71636; SAVERM_3924.
KEGGisma:SAV_3924.
PATRICi23721567. VBIStrAve112782_4186.

Phylogenomic databases

eggNOGiENOG4105E15. Bacteria.
COG2103. LUCA.
HOGENOMiHOG000084045.
KOiK07106.
OMAiAIRIVMQ.
OrthoDBiPOG091H05F1.

Enzyme and pathway databases

UniPathwayiUPA00342.

Family and domain databases

CDDicd05007. SIS_Etherase. 1 hit.
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_STRAW
AccessioniPrimary (citable) accession number: Q82GH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 87 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, Reference 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.