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Protein

Lysozyme M1

Gene

acm

Organism
Streptomyces globisporus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

This enzyme has both lysozyme (acetylmuramidase) and diacetylmuramidase activities.

Catalytic activityi

Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei86PROSITE-ProRule annotation1
Active sitei177PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH25. Glycoside Hydrolase Family 25.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme M1 (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase M1
Gene namesi
Name:acm
OrganismiStreptomyces globisporus
Taxonomic identifieri1908 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_0000018517? – 771 Publication
Signal peptidei1 – ?Sequence analysis
ChainiPRO_000001851878 – 294Lysozyme M1Add BLAST217

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi185 ↔ 2241 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP25310.

Structurei

Secondary structure

1294
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi81 – 87Combined sources7
Helixi89 – 91Combined sources3
Helixi96 – 101Combined sources6
Beta strandi106 – 113Combined sources8
Turni114 – 116Combined sources3
Helixi122 – 131Combined sources10
Beta strandi135 – 141Combined sources7
Turni144 – 146Combined sources3
Helixi149 – 158Combined sources10
Beta strandi166 – 169Combined sources4
Beta strandi173 – 175Combined sources3
Beta strandi180 – 182Combined sources3
Turni184 – 187Combined sources4
Helixi190 – 208Combined sources19
Beta strandi213 – 216Combined sources4
Helixi218 – 225Combined sources8
Turni230 – 234Combined sources5
Beta strandi237 – 240Combined sources4
Beta strandi253 – 255Combined sources3
Beta strandi257 – 267Combined sources11
Beta strandi270 – 281Combined sources12
Helixi283 – 291Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JFXX-ray1.65A78-294[»]
ProteinModelPortaliP25310.
SMRiP25310.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25310.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 25 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR002053. Glyco_hydro_25.
IPR008270. Glyco_hydro_25_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR018077. Glyco_hydro_fam25_subgr.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01183. Glyco_hydro_25. 1 hit.
[Graphical view]
SMARTiSM00641. Glyco_25. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00953. GLYCOSYL_HYDROL_F25. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25310-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAYSSLARR GRRPAVVLLG GLVSASLALT LAPTAAAAPL APPPGKDVGP
60 70 80 90 100
GEAYMGVGTR IEQGLGAGPD ERTIGPADTS GVQGIDVSHW QGSINWSSVK
110 120 130 140 150
SAGMSFAYIK ATEGTNYKDD RFSANYTNAY NAGIIRGAYH FARPNASSGT
160 170 180 190 200
AQADYFASNG GGWSRDNRTL PGVLDIEHNP SGAMCYGLST TQMRTWINDF
210 220 230 240 250
HARYKARTTR DVVIYTTASW WNTCTGSWNG MAAKSPFWVA HWGVSAPTVP
260 270 280 290
SGFPTWTFWQ YSATGRVGGV SGDVDRNKFN GSAARLLALA NNTA
Length:294
Mass (Da):31,169
Last modified:May 1, 1992 - v1
Checksum:iD96EFE914FA04997
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30645 Genomic DNA. Translation: AAA26687.1.
PIRiJQ0529. MUSMM1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30645 Genomic DNA. Translation: AAA26687.1.
PIRiJQ0529. MUSMM1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JFXX-ray1.65A78-294[»]
ProteinModelPortaliP25310.
SMRiP25310.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH25. Glycoside Hydrolase Family 25.

Proteomic databases

PRIDEiP25310.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP25310.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR002053. Glyco_hydro_25.
IPR008270. Glyco_hydro_25_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR018077. Glyco_hydro_fam25_subgr.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF01183. Glyco_hydro_25. 1 hit.
[Graphical view]
SMARTiSM00641. Glyco_25. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00953. GLYCOSYL_HYDROL_F25. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLYSM1_STRGL
AccessioniPrimary (citable) accession number: P25310
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: November 2, 2016
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.