ID   LHYAL_HIRNI             Reviewed;         489 AA.
AC   X4Y2L4;
DT   07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT   11-JUN-2014, sequence version 1.
DT   25-MAY-2022, entry version 20.
DE   RecName: Full=Hyaluronoglucuronidase {ECO:0000305};
DE            Short=LHyal {ECO:0000303|PubMed:24667183};
DE            EC=3.2.1.36 {ECO:0000269|PubMed:24667183};
DE   AltName: Full=Hyaluronate 3-glycanohydrolase {ECO:0000303|PubMed:24667183};
OS   Hirudo nipponia (Korean blood-sucking leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Hirudinida; Hirudiniformes; Hirudinidae; Hirudo.
OX   NCBI_TaxID=42736;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC   TISSUE=Head;
RX   PubMed=24667183; DOI=10.1038/srep04471;
RA   Jin P., Kang Z., Zhang N., Du G., Chen J.;
RT   "High-yield novel leech hyaluronidase to expedite the preparation of
RT   specific hyaluronan oligomers.";
RL   Sci. Rep. 4:4471-4471(2014).
CC   -!- FUNCTION: Hyaluronidase that mediates hydrolysis of (1->3)-linkages
CC       between beta-D-glucuronate and N-acetyl-D-glucosamine residues in
CC       hyaluronate. Very specific to hyaluronate: not able to hydrolyze
CC       chitin, heparin or chondroitin sulfate. {ECO:0000269|PubMed:24667183}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->3)-linkages between beta-D-
CC         glucuronate and N-acetyl-D-glucosamine residues in hyaluronate.;
CC         EC=3.2.1.36; Evidence={ECO:0000269|PubMed:24667183};
CC   -!- ACTIVITY REGULATION: Hyaluronidase activity is inhibited by Mn(2+),
CC       Cu(2+) and Fe(3+). {ECO:0000269|PubMed:24667183}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.5. {ECO:0000269|PubMed:24667183};
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius.
CC         {ECO:0000269|PubMed:24667183};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 79 family. {ECO:0000305}.
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DR   EMBL; KJ026763; AHV78514.1; -; mRNA.
DR   AlphaFoldDB; X4Y2L4; -.
DR   SMR; X4Y2L4; -.
DR   BRENDA; 3.2.1.36; 16673.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0033906; F:hyaluronoglucuronidase activity; IDA:UniProtKB.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030214; P:hyaluronan catabolic process; IDA:UniProtKB.
DR   InterPro; IPR005199; Glyco_hydro_79.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF03662; Glyco_hydro_79n; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Glycosidase; Hydrolase; Transferase.
FT   CHAIN           1..489
FT                   /note="Hyaluronoglucuronidase"
FT                   /id="PRO_0000440625"
FT   ACT_SITE        176
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        290
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   489 AA;  55090 MW;  71CA8A710F8B5F97 CRC64;
     MKEIAVTIDD KNVIASVSES FHGVAFDASL FSPKGLWSFV DITSPKLFKL LEGLSPGYFR
     VGGTFANWLF FDLDENNKWK DYWAFKDKTP ETATITRRWL FRKQNNLKKE TFDDLVKLTK
     GSKMRLLFDL NAEVRTGYEI GKKMTSTWDS SEAEKLFKYC VSKGYGDNID WELGNEPDHT
     SAHNLTEKQV GEDFKALHKV LEKYPTLNKG SLVGPDVGWM GVSYVKGLAD GAGDHVTAFT
     LHQYYFDGNT SDVSTYLDAT YFKKLQQLFD KVKDVLKNSP HKDKPLWLGE TSSGYNSGTK
     DVSDRYVSGF LTLDKLGLSA ANNVKVVIRQ TIYNGYYGLL DKNTLEPNPD YWLMHVHNSL
     VGNTVFKVDV SDPTNKARVY AQCTKTNSKH TQSRYYKGSL TIFALNVGDE DVTLKIDQYS
     GKKIYSYILT PEGGQLTSQK VLLNGKELKL VSDQLPELNA DESKTSFTLS PKTFGFFVVS
     DANVEACKK