ID A0A3B4UTP8_SERDU Unreviewed; 478 AA.
AC A0A3B4UTP8;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
GN Name=SPAM1 {ECO:0000313|Ensembl:ENSSDUP00000021205.1};
OS Seriola dumerili (Greater amberjack) (Caranx dumerili).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Carangiformes; Carangidae; Seriola.
OX NCBI_TaxID=41447 {ECO:0000313|Ensembl:ENSSDUP00000021205.1, ECO:0000313|Proteomes:UP000261420};
RN [1] {ECO:0000313|Ensembl:ENSSDUP00000021205.1}
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; A0A3B4UTP8; -.
DR STRING; 41447.ENSSDUP00000021205; -.
DR GlyCosmos; A0A3B4UTP8; 1 site, No reported glycans.
DR Ensembl; ENSSDUT00000021597.1; ENSSDUP00000021205.1; ENSSDUG00000015441.1.
DR GeneTree; ENSGT01020000230364; -.
DR OMA; RAKIVFE; -.
DR OrthoDB; 5344684at2759; -.
DR Proteomes; UP000261420; 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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..478
FT /note="Hyaluronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017443148"
FT ACT_SITE 136
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT CARBOHYD 359
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT DISULFID 48..342
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 212..228
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 367..378
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 372..427
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 429..435
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ SEQUENCE 478 AA; 55626 MW; 27A6B9BD424114E3 CRC64;
MNRVKLQFSV FITMLALLSS GRALPRTDPP IRPGHPFLFM WNAPTELCDI RFAMPLDLSY
FHFVSSTLKT ATNQSISIFY TDRFGIFPYV DEDTGEMYDE GLPQLIDLQE HHELAEDDIE
YYIPGDQPGL AVLDFEEWRP QWVRNWGSKD IYRQISIETV KKKNTTLSDN EAEDRAKIVF
ERAAMRYFLR SIRIGKRLRP NRLWGYYLYP DCYNYDYNQD MAGFTGECPA IEKDRNDELL
WLWRDSTALF PSIYLELTLR DSQQARLFVR HRIQEAIRVS SLPNSSYSIP VYAYIRPVYK
DSIDDYMSEF DLVNTIGEAA ALGAAGVVSW GDMNVTDTED SCFDARRHLE QVMNPYIVNV
STATHLCSQA LCQGRGRCVR KRWDDDVFLH LDPHRYRIQR QRRGGPLTVS GGLSQDDINW
FDRSFDCMCY SEEPCRSPLT INVIQEAVFT RRSRGADRPR PLPLVMTLLC LTYVWINI
//
