ID   A0A3B4FZN9_9CICH        Unreviewed;       408 AA.
AC   A0A3B4FZN9;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE            EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
OS   Pundamilia nyererei.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX   NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000014786.1, ECO:0000313|Proteomes:UP000261460};
RN   [1] {ECO:0000313|Ensembl:ENSPNYP00000014786.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-
CC         glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35;
CC         Evidence={ECO:0000256|ARBA:ARBA00000251,
CC         ECO:0000256|RuleBase:RU610713};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {ECO:0000256|ARBA:ARBA00008871, ECO:0000256|PIRNR:PIRNR038193,
CC       ECO:0000256|RuleBase:RU610713}.
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DR   AlphaFoldDB; A0A3B4FZN9; -.
DR   Ensembl; ENSPNYT00000015165.1; ENSPNYP00000014786.1; ENSPNYG00000011025.1.
DR   GeneTree; ENSGT01020000230364; -.
DR   Proteomes; UP000261460; Unplaced.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR018155; Hyaluronidase.
DR   PANTHER; PTHR11769; HYALURONIDASE; 1.
DR   PANTHER; PTHR11769:SF36; HYALURONIDASE; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 2.
DR   PIRSF; PIRSF038193; Hyaluronidase; 2.
DR   PRINTS; PR00846; GLHYDRLASE56.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR038193-3};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU610713};
KW   Hydrolase {ECO:0000256|RuleBase:RU610713};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..408
FT                   /note="Hyaluronidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017486522"
FT   CARBOHYD        323
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT   DISULFID        200..217
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT   DISULFID        331..342
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ   SEQUENCE   408 AA;  46001 MW;  E7EDF1D364FCD78C CRC64;
     RATVALFFLM IAAFAGICTA APPRPAFPPL LSGQPFIIFW GIPDSSCSGR PDPGSFGMER
     DSRVAVFYED TLGNYPYFVD IDTPINGGLP QHTRLETHLQ KMKQDLEEAL PAPRYLGLGV
     LRWGEWVPQW SRSREKQALY VEASKKLLKG FFPNWTPAEV EKWSKVDFEA AAQSVMMETL
     REVKKLRPKA LWGFSPYPSC YNSDPTQTML ANYTGQCPPA EMALNDELSW LWKRSSALYP
     LLTLEKLQVS NFSTHCIDLS WLNLLHIFFV FLLQADLVSS VGESAAMGTA GVVVWERSEI
     KTEVHTVKKH WLSLNVLGPY SINVTTAARL CSASLCQGRG RCVRQNPESS AYLHLPPPSR
     QFYTNSHHNQ LNVFFGLIFT ALMITSAERH RGARFAELMR CSELHIHI
//