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Reviewed, UniProtKB/Swiss-Prot Q59634 (HYSA_PROAC)

Last modified June 16, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
Ordered Locus Names: PPA0380
OrganismPropionibacterium acnes [Complete proteome] [HAMAP]
Taxonomic identifier1747 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesPropionibacterineaePropionibacteriaceaePropionibacterium

Protein attributes

Sequence length813 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 649 and 779.

Ontologies

Keywords
   Cellular componentCell wall
Secreted
   DomainSignal
   Molecular functionLyase
   Technical termComplete proteome
Direct 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-SubCell

   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 – 3232Tat-type signal
Chain33 – 813781Hyaluronate lyase
PRO_0000024930

Experimental info

Sequence conflict2041A → G in AAA51650. Ref.1
Sequence conflict3041V → D in AAA51650. Ref.1
Sequence conflict405 – 42521RPVPE…RLVHR → PRPGVVDAELLRVHGPSRPA in AAA51650. Ref.1
Sequence conflict4541S → Y in AAA51650. Ref.1
Sequence conflict649 – 6579VTHHDRPVA → GHPPRSSSP in AAA51650. Ref.1
Sequence conflict688 – 6947ATVQAVR → GNRPGRA in AAA51650. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q59634-1 [UniParc].

Last modified September 27, 2004. Version 2.
Checksum: 0C4316E7890D4D1D

FASTA81388,130
        10         20         30         40         50         60 
MFGTPSRRTF LTASALSAMA LAASPTVTDA IAAPGPDSWS ALCERWIDII TGRRAARTSD 

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

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

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

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

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

       370        380        390        400        410        420 
ALPTHRAEQW RGIVHGWMAR NTFDHLSEPS TLVDISLFDA AAKARPVPES STPSYFASMD 

       430        440        450        460        470        480 
RLVHRTADWL ITVSNCSDRI AWYEYGNGEN EWASRTSQGM RYLLLPGDMG QYEDGYWATV 

       490        500        510        520        530        540 
DYSAPTGTTV DSTPLKRAVG ASWAAKTPTN EWSGGLASGS WSAAASHITS QDSALKARRL 

       550        560        570        580        590        600 
WVGLKDAMVE LTTDVTTDAS RAITVVEHRK VASSSTKLLV DGNRVSSATS FQNPRWAHLD 

       610        620        630        640        650        660 
GVGGYVFATD TDLSADVATR KGTWIDVNPS RKVKGADEVI ERAYASLHVT HHDRPVAWAL 

       670        680        690        700        710        720 
LPTASRSHTM ALATRPGVEP FTVLRNDATV QAVRSAGALL TKDPTVVTTL AFWKPATCGG 

       730        740        750        760        770        780 
VAVNRPALVQ TRESANQMEV VIVEPTQKRG SLTVTIEGSW KVKTADSHVD VSCENAAGTL 

       790        800        810 
HVDTAGLGGQ SVRVTLARQV TQTPSGGGRH DRA 

« Hide

References

« Hide 'large scale' 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: 9115089] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"The complete genome sequence of Propionibacterium acnes, a commensal of human skin."
Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G.
Science 305:671-673(2004) [PubMed: 15286373] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases

U15927 Genomic DNA. Translation: AAA51650.1. Frameshift.
AE017283 Genomic DNA. Translation: AAT82132.1.
RefSeqYP_055090.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

CAZyPL8. Polysaccharide Lyase Family 8.

Genome annotation databases

GeneID2932015.
GenomeReviewsGene locus PPA0380 in contig AE017283_GR.
KEGGpac:PPA0380.
NMPDRfig|267747.1.peg.367.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ59634.
OMAQ59634. SRINESA.

Enzyme and pathway databases

BioCycPACN267747:PPA0380-MON.
BRENDA4.2.2.1. 39123.

Family and domain databases

InterProIPR014718. Glyco_hydro-type_carb-bd_sub.
IPR012970. Lyase_8_alpha_N.
IPR004103. Lyase_8_C.
IPR003159. Lyase_8_central.
IPR012329. Lyase_8_N.
IPR006311. Tat.
IPR017909. Twin_arg_translocation_Tat.
[Graphical view]
Gene3DG3DSA:2.70.98.10. Glyco_hydro_42_D5. 1 hit.
G3DSA:2.60.220.10. Lyase_8_C. 1 hit.
G3DSA:1.50.10.100. Lyase_8_N. 1 hit.
PfamPF02278. Lyase_8. 1 hit.
PF02884. Lyase_8_C. 1 hit.
PF08124. Lyase_8_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01409. TAT_signal_seq. 1 hit.
PROSITEPS51318. TAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHYSA_PROAC
AccessionPrimary (citable) accession number: Q59634
Secondary accession number(s): Q6AAT4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: September 27, 2004
Last modified: June 16, 2009
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents