ID A0A3B3T657_9TELE Unreviewed; 492 AA.
AC A0A3B3T657;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
OS Paramormyrops kingsleyae.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Osteoglossocephala;
OC Osteoglossomorpha; Osteoglossiformes; Mormyridae; Paramormyrops.
OX NCBI_TaxID=1676925 {ECO:0000313|Ensembl:ENSPKIP00000037953.1, ECO:0000313|Proteomes:UP000261540};
RN [1] {ECO:0000313|Ensembl:ENSPKIP00000037953.1}
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; A0A3B3T657; -.
DR STRING; 1676925.ENSPKIP00000037953; -.
DR Ensembl; ENSPKIT00000018940.1; ENSPKIP00000037953.1; ENSPKIG00000015917.1.
DR GeneTree; ENSGT01020000230364; -.
DR Proteomes; UP000261540; 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..42
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 43..492
FT /note="Hyaluronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017390413"
FT ACT_SITE 156
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT DISULFID 69..354
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 232..246
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 379..390
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 384..437
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 439..445
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ SEQUENCE 492 AA; 54089 MW; 3B77A3B2771221D8 CRC64;
MFTVLHSYTK GVNMSYCTPA WRRRPLLSSV LCLVLLETLG AAQLLPPAAA PLFDGQPFVA
AWNVPTGVCQ RLGVALDMAP FQLVTTPAKV VGQPLMLFYS DRLGLYPRVD AITHSLLHGG
IPQRGDLRAS LAKARADIAH YITATTAPGL AVIDWEDWRP VWERNWGPKS IYRSLSVSHA
RQRYPFLSPE QTVRVARRHF QAAARSYMCA TLSLATKLRP NYQWGYYLYP NCYNYGWEEA
GYTGRCPPEV VQQNDDLGWL WQSSTALFPS VYLTASLGGG SHTALFVRHR VQEAMRTAAL
ARPAAALPVY VYTRPVFVDQ NRRFLSQADL VSCIGESAAA GASGSVLWGA SASCEALSAY
LSSTLGPYVA NVTAAARLCS AVLCQGHGRC LRRRRDTDDH LHLNPASFSI LRSEGGYLAV
GSLTASDLAK LADKFTCQCY AGRSCSSEIS PEDPGSVWAC YLCLLYVFSC SHMICCLREQ
AAYFHQQVCL LN
//
