ID A0A401Q5F7_SCYTO Unreviewed; 348 AA.
AC A0A401Q5F7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
GN ORFNames=scyTo_0016262 {ECO:0000313|EMBL:GCB80577.1};
OS Scyliorhinus torazame (Cloudy catshark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Elasmobranchii; Galeomorphii; Galeoidea; Carcharhiniformes; Scyliorhinidae;
OC Scyliorhinus.
OX NCBI_TaxID=75743 {ECO:0000313|EMBL:GCB80577.1, ECO:0000313|Proteomes:UP000288216};
RN [1] {ECO:0000313|EMBL:GCB80577.1, ECO:0000313|Proteomes:UP000288216}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=30297745; DOI=.1038/s41559-018-0673-5;
RA Hara Y, Yamaguchi K, Onimaru K, Kadota M, Koyanagi M, Keeley SD, Tatsumi K,
RA Tanaka K, Motone F, Kageyama Y, Nozu R, Adachi N, Nishimura O, Nakagawa R,
RA Tanegashima C, Kiyatake I, Matsumoto R, Murakumo K, Nishida K, Terakita A,
RA Kuratani S, Sato K, Hyodo S Kuraku.S.;
RT "Shark genomes provide insights into elasmobranch evolution and the origin
RT of vertebrates.";
RL Nat. Ecol. Evol. 2:1761-1771(2018).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCB80577.1}.
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DR EMBL; BFAA01009716; GCB80577.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401Q5F7; -.
DR STRING; 75743.A0A401Q5F7; -.
DR OMA; ICEERFN; -.
DR Proteomes; UP000288216; Unassembled WGS sequence.
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:SF35; HYALURONIDASE; 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 Reference proteome {ECO:0000313|Proteomes:UP000288216};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..348
FT /note="Hyaluronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019278937"
FT ACT_SITE 139
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT DISULFID 215..231
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ SEQUENCE 348 AA; 39534 MW; 4231BED1E861297D CRC64;
MLPGLILPAC TLFYFSIQPA IIWGVEVKTT LASPMIYNKP FTVVWNTPIA KCKTKYDVTL
DLSAFDIVQN ENGLLMGKKI TLFDKKQLGL YPYYTAEGTP VNGGLVQNAS LSRHLEVSTT
DIDKVMDQDF SGLAVVDWED WRPLWVRNWG SMDIYRKKSV ELEKSKNTDL PESEILPIAK
NKYETAAQNF MSQTLELGKT LRSKSYWGFY LFPDCYNYFK ANEQTGYTGQ CSEVDIPRNN
QLAWLWKVSQ CLYPSVYIAQ GAEPVTVQKF VHYRVKEALR VAALGRSNEA LPVLVYGRYS
YRHTLDFLSE IDLVHTIGES AAMGASGMVL WGNNYYARTM VSISFPNM
//
