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P0CZ00 (HYSA_PROAA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 10. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Hyaluronate lyase

EC=4.2.2.1
Alternative name(s):
Hyaluronidase
Short name=HYase
OrganismPropionibacterium acnes
Taxonomic identifier1747 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium

Protein attributes

Sequence length812 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.

Subunit structure

Monomer.

Subcellular location

Secretedcell wall.

Post-translational modification

Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.

Sequence similarities

Belongs to the polysaccharide lyase 8 family.

Sequence caution

The sequence AAA51650.1 differs from that shown. Reason: Frameshift at positions 717 and 778.

Ontologies

Keywords
   Cellular componentCell wall
Secreted
   DomainSignal
   Molecular functionLyase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

hyaluronate lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232Tat-type signal
Chain33 – 812780Hyaluronate lyase
PRO_0000410486

Sequences

Sequence LengthMass (Da)Tools
P0CZ00 [UniParc].

Last modified June 28, 2011. Version 1.
Checksum: D72FB62E1439CB96

FASTA81287,758
        10         20         30         40         50         60 
MFGTPSRRTF LTASALSAMA LAASPTVTDA IAAPGPDSWS ALCERWIDII TGRRAARTSD 

        70         80         90        100        110        120 
PRARAIIAKT DRKVAEILTD LVSGSSRQTV LISADLRKEQ SPFITKTARA IESMACGWAT 

       130        140        150        160        170        180 
PGSSYHKDPE ILSACIEGLR DFCRLRYNPS QDEYGNWWDW EDGASRAVAD VMCILHDVLP 

       190        200        210        220        230        240 
PEVMSAAAAG IDHFIPDPWF QQPGSVKPTA NPVQPVVSTG ANRMDLTRAV MCRSIATGDE 

       250        260        270        280        290        300 
KRLRHAVDGL PDAWRVTTEG DGFRADGGFI QHSHIPYTGG YGDVLFSGLA MLFPLVSGMR 

       310        320        330        340        350        360 
FDIDESARKA FHDQVERGFI PVMYNGQILD DVRGRSISRI NESAAMHGIS IARAMLMMAD 

       370        380        390        400        410        420 
ALPTHRAEQW RGIVHGWMAR NTFDHLSEPS TLVDISLFDA AAKAPRPGVV DAELLRVHGP 

       430        440        450        460        470        480 
SRPATADWLI TVSNCSDRIA WYEYGNGENE WAYRTSQGMR YLLLPGDMGQ YEDGYWATVD 

       490        500        510        520        530        540 
YSAPTGTTVD STPLKRAVGA SWAAKTPTNE WSGGLASGSW SAAASHITSQ DSALKARRLW 

       550        560        570        580        590        600 
VGLKDAMVEL TTDVTTDASR AITVVEHRKV ASSSTKLLVD GNRVSSATSF QNPRWAHLDG 

       610        620        630        640        650        660 
VGGYVFATDT DLSADVATRK GTWIDVNPSR KVKGADEVIE RAYASLHGHP PRSSSPWALL 

       670        680        690        700        710        720 
PTASRSHTMA LATRPGVEPF TVLRNDGNRP GRASAGALLT KDPTVVTTLA FWKPATCGGV 

       730        740        750        760        770        780 
AVNRPALVQT RESANQMEVV IVEPTQKRGS LTVTIEGSWK VKTADSHVDV SCENAAGTLH 

       790        800        810 
VDTAGLGGQS VRVTLARQVT QTPSGGGRHD RA 

« Hide

References

[1]"Cloning and sequencing of the hyaluronate lyase gene from Propionibacterium acnes."
Steiner B.M., Romero-Steiner S., Cruce D., George R.
Can. J. Microbiol. 43:315-321(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: 49/51.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U15927 Genomic DNA. Translation: AAA51650.1. Frameshift.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA4.2.2.1. 5029.

Family and domain databases

Gene3D1.50.10.100. 1 hit.
2.60.220.10. 1 hit.
2.70.98.10. 1 hit.
InterProIPR008929. Chondroitin_lyas.
IPR011013. Gal_mutarotase_SF_dom.
IPR014718. Glyco_hydro-type_carb-bd_sub.
IPR011071. Lyase_8-like_C.
IPR012970. Lyase_8_alpha_N.
IPR004103. Lyase_8_C.
IPR003159. Lyase_8_central_dom.
IPR012329. Lyase_8_N.
IPR006311. TAT_signal.
[Graphical view]
PfamPF02278. Lyase_8. 1 hit.
PF02884. Lyase_8_C. 1 hit.
PF08124. Lyase_8_N. 1 hit.
[Graphical view]
SUPFAMSSF48230. SSF48230. 1 hit.
SSF49863. SSF49863. 1 hit.
SSF74650. SSF74650. 1 hit.
PROSITEPS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHYSA_PROAA
AccessionPrimary (citable) accession number: P0CZ00
Secondary accession number(s): Q59634, Q6AAT4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 28, 2011
Last sequence update: June 28, 2011
Last modified: October 16, 2013
This is version 10 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families