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Q90VZ3

- LYG_PAROL

UniProt

Q90VZ3 - LYG_PAROL

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Protein

Lysozyme g

Gene
N/A
Organism
Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Possesses lytic activity against M.lysodeikticus and several fish pathogenic bacteria.

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.

pH dependencei

Optimum pH is 6.0.

Temperature dependencei

Optimum temperature is 25 degrees Celsius.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei71 – 711By similarity
Active sitei84 – 841By similarity

GO - Molecular functioni

  1. lysozyme activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall macromolecule catabolic process Source: InterPro
  2. cytolysis Source: UniProtKB-KW
  3. defense response to bacterium Source: UniProtKB-KW
  4. peptidoglycan catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH23. Glycoside Hydrolase Family 23.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme g (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase
OrganismiParalichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus)
Taxonomic identifieri8255 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataCarangariaPleuronectiformesPleuronectoideiParalichthyidaeParalichthys

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 195195Lysozyme gPRO_0000193520Add
BLAST

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ90VZ3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 23 family.Curated

Phylogenomic databases

HOVERGENiHBG006299.

Family and domain databases

InterProiIPR002152. Glyco_hydro_23.
IPR023346. Lysozyme-like_dom.
IPR008258. TGlycosylase-like_SLT.
[Graphical view]
PfamiPF01464. SLT. 1 hit.
[Graphical view]
PIRSFiPIRSF001065. Lysozyme_g. 1 hit.
PRINTSiPR00749. LYSOZYMEG.
SUPFAMiSSF53955. SSF53955. 1 hit.

Sequencei

Sequence statusi: Complete.

Q90VZ3-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSYGQIRLVE TSGASGATSQ QDNLGYSGVK ASHKMAEIDS GRMSKYKSKI
60 70 80 90 100
NKVGQSYGIE PALIAAIISR ESRAGNQLKD GWGDWNPQRQ AYNAWGLMQV
110 120 130 140 150
DVNPNGGGHT AVGGWDSEDH LRQATGILVT FIERIRTKFP GWSKEKQLKG
160 170 180 190
GIAAYNMGDK NVHSYEGVDE NTTGRDYSND VTARAQWYRD NGYSG
Length:195
Mass (Da):21,385
Last modified:December 1, 2001 - v1
Checksum:i511DAF31876F662F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB050591 Genomic DNA. Translation: BAB62407.1.
AB050590 mRNA. Translation: BAB62406.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB050591 Genomic DNA. Translation: BAB62407.1 .
AB050590 mRNA. Translation: BAB62406.1 .

3D structure databases

ProteinModelPortali Q90VZ3.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH23. Glycoside Hydrolase Family 23.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

HOVERGENi HBG006299.

Family and domain databases

InterProi IPR002152. Glyco_hydro_23.
IPR023346. Lysozyme-like_dom.
IPR008258. TGlycosylase-like_SLT.
[Graphical view ]
Pfami PF01464. SLT. 1 hit.
[Graphical view ]
PIRSFi PIRSF001065. Lysozyme_g. 1 hit.
PRINTSi PR00749. LYSOZYMEG.
SUPFAMi SSF53955. SSF53955. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning, expression and evolution of the Japanese flounder goose-type lysozyme gene, and the lytic activity of its recombinant protein."
    Hikima J., Minagawa S., Hirono I., Aoki T.
    Biochim. Biophys. Acta 1520:35-44(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], CHARACTERIZATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiLYG_PAROL
AccessioniPrimary (citable) accession number: Q90VZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: December 1, 2001
Last modified: October 29, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3