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Reviewed, UniProtKB/Swiss-Prot Q53591 (HYSA_STRA3)

Last modified November 25, 2008. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Hyaluronate lyase
    EC=4.2.2.1
Alternative name(s):
    Hyaluronidase
      Short name=HYase
Gene names
Name: hylB
Ordered Locus Names: gbs1270
OrganismStreptococcus agalactiae serotype III [Complete proteome] [HAMAP]
Taxonomic identifier216495 [NCBI]
Taxonomic lineageBacteriaFirmicutesLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length984 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine.

Subcellular location

Secreted.

Sequence similarities

Belongs to the polysaccharide lyase 8 family.

Ontologies

Keywords

   Cellular componentSecreted
   DomainSignal
   Molecular functionLyase
   Technical term3D-structure
Complete proteome

Gene Ontology (GO)

   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: InterPro

   Molecular functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

hyaluronate lyase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 4040 Potential
Chain41 – 984944Hyaluronate lyase
PRO_0000024932

Sites

Active site4291
Active site4791
Active site4881

Experimental info

Sequence conflict451E → G in AAA56749. Ref.1
Sequence conflict155 – 1562SA → FV in AAA56749. Ref.1
Sequence conflict1831E → K in AAA56749. Ref.1
Sequence conflict246 – 2516ASTEDK → GSPEDN in AAA56749. Ref.1
Sequence conflict2671H → Y in AAA56749. Ref.1
Sequence conflict279 – 2802IN → LT in AAA56749. Ref.1
Sequence conflict2881A → G in AAA56749. Ref.1
Sequence conflict292 – 2932KT → EA in AAA56749. Ref.1
Sequence conflict3001H → R in AAA56749. Ref.1
Sequence conflict3841A → G in AAA56749. Ref.1
Sequence conflict3871A → S in AAA56749. Ref.1
Sequence conflict4131G → E in AAA56749. Ref.1
Sequence conflict4201D → V in AAA56749. Ref.1
Sequence conflict5831T → A in AAA56749. Ref.1
Sequence conflict6091M → L in AAA56749. Ref.1
Sequence conflict6391E → K in AAA56749. Ref.1
Sequence conflict6661D → G in AAA56749. Ref.1
Sequence conflict6761L → I in AAA56749. Ref.1
Sequence conflict688 – 6892FW → LG in AAA56749. Ref.1
Sequence conflict8821Q → L in AAA56749. Ref.1
Sequence conflict8941M → L in AAA56749. Ref.1

Secondary structure

................................................................................................................................. 984
Helix Strand Turn

Details...