ID A0A3B4FWZ5_9CICH Unreviewed; 439 AA.
AC A0A3B4FWZ5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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:ENSPNYP00000014269.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000014269.1}
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; A0A3B4FWZ5; -.
DR Ensembl; ENSPNYT00000014627.1; ENSPNYP00000014269.1; ENSPNYG00000010633.1.
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:SF20; HYALURONIDASE PH-20; 1.
DR Pfam; PF01630; Glyco_hydro_56; 1.
DR PIRSF; PIRSF038193; Hyaluronidase; 1.
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..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..439
FT /note="Hyaluronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017397455"
FT ACT_SITE 134
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT DISULFID 47..333
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 210..224
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 358..369
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 363..416
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 418..424
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ SEQUENCE 439 AA; 49624 MW; 5C2024745C09DA30 CRC64;
MAPSFFSSVG FCVIGSITLA LALPPTEPPL INDHSFVAIW NAPVEHCKRL HIPLDTAAFQ
SVTTPAAVPG QFLTIFYEDR LGHYPRADSV KHKLYSGGVP QNGNLTEHLA RAQKQIDHYI
SQDSSPGLAV IDWESWRPLW DQNWGSKRIY QKLSISHTLQ MLPFLSLEQI LKLAKKQFQR
AGRHFMEKTI SLGTGERPNR RWGFYLFPDC YNYGWNKLGY TGECSHKTHK QNNQMLWLWE
RSTALFPSVY LHQNLRNSPQ AALFVRNRVL EALRVAALPK RPYVMPVYVY CRPLYRDQTK
KDLISTIGES AALGASGVII WGDGLTATIH ASCDALSKYL RSTLNPYIAN VTAAAKLCSE
VLCQGKGRCV RKSNNSRHYL HLNPTHFHII RADRKYVAIG LPSAADLSAW AENFTCQCYA
GRNCSPKLVH PTTMKLIWI
//
