murQ

Functionⁱ

Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate. Is required for growth on MurNAc as the sole source of carbon and energy. 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.2 Publications

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.

Catalytic activityⁱ

(R)-lactate + N-acetyl-D-glucosamine 6-phosphate = N-acetylmuramate 6-phosphate + H₂O.1 Publication

Kineticsⁱ

kcat is 5.7 s(-1).

K_M=
1.20 mM for N-acetylmuramic acid 6-phosphate
1 Publication
Manual assertion based on experiment inⁱ
- Ref.7
  "Mechanistic studies on N-acetylmuramic acid 6-phosphate hydrolase (MurQ): an etherase involved in peptidoglycan recycling."
  Hadi T., Dahl U., Mayer C., Tanner M.E.
  Biochemistry 47:11547-11558(2008) [PubMed] [Europe PMC] [Abstract]
  Cited for: KINETIC PARAMETERS, SUBUNIT, REACTION MECHANISM, ACTIVE SITE, MUTAGENESIS OF GLU-83; GLU-114 AND ASP-115.

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.
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.
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.
View all proteins of this organism that are known to be involved in the pathway peptidoglycan recycling and in Cell wall biogenesis.

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Active siteⁱ	83	Proton donor1 Publication		1
Active siteⁱ	114	1 Publication		1

GO - Molecular functionⁱ

carbohydrate derivative binding Source: InterPro
carbon-oxygen lyase activity
Source: EcoCyc
Inferred from direct assayⁱ
- 15983044
ether hydrolase activity
Source: EcoliWiki
Inferred from direct assayⁱ
- 18837509

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

1,6-anhydro-N-acetyl-beta-muramic acid catabolic process Source: UniProtKB-UniPathway
amino sugar catabolic process
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 15983044
carbohydrate metabolic process Source: UniProtKB-KW
N-acetylmuramic acid catabolic process Source: UniProtKB-UniPathway
peptidoglycan turnover
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 16452451

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Lyase
Biological process	Carbohydrate metabolism

Enzyme and pathway databases

BioCycⁱ	EcoCyc:G7263-MONOMER MetaCyc:G7263-MONOMER
UniPathwayⁱ	UPA00342 UPA00343 UPA00544

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: N-acetylmuramic acid 6-phosphate etherase (EC:4.2.1.126) Short name: MurNAc-6-P etherase Alternative name(s): N-acetylmuramic acid 6-phosphate hydrolase N-acetylmuramic acid 6-phosphate lyase
Gene namesⁱ	Name:murQ Synonyms:yfeU Ordered Locus Names:b2428, JW2421
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG14162 murQ

EcoGeneⁱ

EG14162 murQ

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	83	E → A: 10000-fold reduction in catalytic activity. 1 Publication	1
Mutagenesisⁱ	83	E → Q: Loss of catalytic activity. 1 Publication	1
Mutagenesisⁱ	114	E → Q: 2000-fold reduction in catalytic activity and 4-fold increase in substrate affinity. 1 Publication	1
Mutagenesisⁱ	115	D → N: 7-fold reduction in catalytic activity and 1.5-fold increase in substrate affinity. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000214829	1 – 298	N-acetylmuramic acid 6-phosphate etheraseAdd BLAST		298

Proteomic databases

EPDⁱ	P76535
PaxDbⁱ	P76535
PRIDEⁱ	P76535

Expressionⁱ

Inductionⁱ

Induced by MurNAc 6-phosphate that releases the repressor MurR from the DNA. Also up-regulated by the cAMP receptor protein crp via the binding of crp-cAMP to a class I site upstream of the murQ promoter. Repressed by MurR in the absence of MurNAc 6-phosphate.1 Publication

Interactionⁱ

Subunit structureⁱ

Homodimer.1 Publication

Protein-protein interaction databases

BioGridⁱ	4260569, 7 interactors
IntActⁱ	P76535, 6 interactors
STRINGⁱ	316385.ECDH10B_2593

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P76535
SMRⁱ	P76535
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	55 – 218	SISAdd BLAST		164

Sequence similaritiesⁱ

Belongs to the GCKR-like family. MurNAc-6-P etherase subfamily.Curated

Phylogenomic databases

eggNOGⁱ	ENOG4105E15 Bacteria COG2103 LUCA
HOGENOMⁱ	HOG000084045
InParanoidⁱ	P76535
KEGG Orthology (KO) More...KOⁱ	K07106
PhylomeDBⁱ	P76535

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd05007 SIS_Etherase, 1 hit
HAMAPⁱ	MF_00068 MurQ, 1 hit
InterProⁱ	View protein in InterPro IPR005488 Etherase_MurQ IPR005486 Glucokinase_regulatory_CS IPR001347 SIS
PANTHERⁱ	PTHR10088:SF5 PTHR10088:SF5, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF01380 SIS, 1 hit
TIGRFAMsⁱ	TIGR00274 TIGR00274, 1 hit
PROSITEⁱ	View protein in PROSITE PS01272 GCKR, 1 hit PS51464 SIS, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P76535-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MQFEKMITEG SNTASAEIDR VSTLEMCRII NDEDKTVPLA VERVLPDIAA 
        60         70         80         90        100
AIDVIHAQVS GGGRLIYLGA GTSGRLGILD ASECPPTYGV KPGLVVGLIA 
       110        120        130        140        150
GGEYAIQHAV EGAEDSREGG VNDLKNINLT AQDVVVGIAA SGRTPYVIAG 
       160        170        180        190        200
LEYARQLGCR TVGISCNPGS AVSTTAEFAI TPIVGAEVVT GSSRMKAGTA 
       210        220        230        240        250
QKLVLNMLST GLMIKSGKVF GNLMVDVVAT NEKLHVRQVN IVKNATGCSA 
       260        270        280        290 
EQAEAALIAC ERNCKTAIVM VLKNLDAAEA KKRLDQHGGF IRQVLDKE

Length:298

Mass (Da):31,220

Last modified:February 1, 1997 - v1

Checksum:ⁱ34FE8F878E8B3077

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U00096 Genomic DNA Translation: AAC75481.1 AP009048 Genomic DNA Translation: BAA16312.2
PIRⁱ	C65017
NCBI Reference Sequences More...RefSeqⁱ	NP_416923.1, NC_000913.3 WP_001159160.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC75481; AAC75481; b2428 BAA16312; BAA16312; BAA16312
GeneIDⁱ	946893
KEGGⁱ	ecj:JW2421 eco:b2428
PATRICⁱ	fig\|1411691.4.peg.4303

Protein	Similar proteins		Species	Score	Length	Source
P76535	N-acetylmuramic acid 6-phosphate etherase		ECOBW		298	UniRef100_C4ZVV9
N-acetylmuramic acid 6-phosphate etherase		ECODH		298
N-acetylmuramic acid 6-phosphate etherase		ECOHS		298
N-acetylmuramic acid 6-phosphate etherase		ECOLC		298
N-acetylmuramic acid 6-phosphate etherase		Shigella sp.		298
+25

Protein	Similar proteins		Species	Score	Length	Source
P76535	N-acetylmuramic acid 6-phosphate etherase		ECO57		298	UniRef90_Q8XBJ2
N-acetylmuramic acid 6-phosphate etherase		ECO5E		298
N-acetylmuramic acid 6-phosphate etherase		ECO24		298
N-acetylmuramic acid 6-phosphate etherase		ECO55		298
N-acetylmuramic acid 6-phosphate etherase		ECO8A		298
+579

Protein	Similar proteins		Species	Score	Length	Source
P76535	N-acetylmuramic acid 6-phosphate etherase 2		VIBCH		307	UniRef50_Q9KU39
N-acetylmuramic acid 6-phosphate etherase		ECOLU		298
N-acetylmuramic acid 6-phosphate etherase		SHIDS		298
N-acetylmuramic acid 6-phosphate etherase		ECO57		298
N-acetylmuramic acid 6-phosphate etherase		ECO5E		298
+2357

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U00096 Genomic DNA Translation: AAC75481.1 AP009048 Genomic DNA Translation: BAA16312.2
PIRⁱ	C65017
RefSeqⁱ	NP_416923.1, NC_000913.3 WP_001159160.1, NZ_LN832404.1

3D structure databases

ProteinModelPortalⁱ	P76535
SMRⁱ	P76535
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4260569, 7 interactors
IntActⁱ	P76535, 6 interactors
STRINGⁱ	316385.ECDH10B_2593

Proteomic databases

EPDⁱ	P76535
PaxDbⁱ	P76535
PRIDEⁱ	P76535

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC75481; AAC75481; b2428 BAA16312; BAA16312; BAA16312
GeneIDⁱ	946893
KEGGⁱ	ecj:JW2421 eco:b2428
PATRICⁱ	fig\|1411691.4.peg.4303

Organism-specific databases

EchoBASEⁱ	EB3914
EcoGeneⁱ	EG14162 murQ

Phylogenomic databases

eggNOGⁱ	ENOG4105E15 Bacteria COG2103 LUCA
HOGENOMⁱ	HOG000084045
InParanoidⁱ	P76535
KOⁱ	K07106
PhylomeDBⁱ	P76535

Enzyme and pathway databases

UniPathwayⁱ	UPA00342 UPA00343 UPA00544
BioCycⁱ	EcoCyc:G7263-MONOMER MetaCyc:G7263-MONOMER

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P76535

PROⁱ

PR:P76535

Family and domain databases

CDDⁱ	cd05007 SIS_Etherase, 1 hit
HAMAPⁱ	MF_00068 MurQ, 1 hit
InterProⁱ	View protein in InterPro IPR005488 Etherase_MurQ IPR005486 Glucokinase_regulatory_CS IPR001347 SIS
PANTHERⁱ	PTHR10088:SF5 PTHR10088:SF5, 1 hit
Pfamⁱ	View protein in Pfam PF01380 SIS, 1 hit
TIGRFAMsⁱ	TIGR00274 TIGR00274, 1 hit
PROSITEⁱ	View protein in PROSITE PS01272 GCKR, 1 hit PS51464 SIS, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MURQ_ECOLI
Accessionⁱ	P76535Primary (citable) accession number: P76535 Secondary accession number(s): P76965, P76966, P76967
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
	Last sequence update:	February 1, 1997
	Last modified:	November 7, 2018
	This is version 135 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
PATHWAY comments
Index of metabolic and biosynthesis pathways
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P76535 (MURQ_ECOLI)

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N-acetylmuramic acid 6-phosphate etherase

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: 1,6-anhydro-N-acetylmuramate degradation

Pathwayi: N-acetylmuramate degradation

Pathwayi: peptidoglycan recycling

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

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Functionⁱ

Kineticsⁱ

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

Pathwayⁱ: N-acetylmuramate degradation

Pathwayⁱ: peptidoglycan recycling

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ