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Database: UniProt
Entry: A0A093ENP7_TYTAL
LinkDB: A0A093ENP7_TYTAL
Original site: A0A093ENP7_TYTAL 
ID   A0A093ENP7_TYTAL        Unreviewed;       403 AA.
AC   A0A093ENP7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   13-FEB-2019, entry version 12.
DE   RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE            EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
DE   AltName: Full=Hyaluronoglucosaminidase {ECO:0000256|RuleBase:RU610713};
DE   Flags: Fragment;
GN   ORFNames=N341_01062 {ECO:0000313|EMBL:KFV46952.1};
OS   Tyto alba (Barn owl).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Strigiformes; Tytonidae; Tyto.
OX   NCBI_TaxID=56313 {ECO:0000313|EMBL:KFV46952.1};
RN   [1] {ECO:0000313|EMBL:KFV46952.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N341 {ECO:0000313|EMBL:KFV46952.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-
CC         beta-D-glucosamine and D-glucuronate residues in hyaluronate.;
CC         EC=3.2.1.35; Evidence={ECO:0000256|RuleBase:RU610713};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 56 family.
CC       {ECO:0000256|RuleBase:RU610713}.
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DR   EMBL; KK378052; KFV46952.1; -; Genomic_DNA.
DR   GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR018155; Hyaluronidase.
DR   PANTHER; PTHR11769; PTHR11769; 1.
DR   Pfam; PF01630; Glyco_hydro_56; 1.
DR   PIRSF; PIRSF038193; Hyaluronidase; 1.
DR   PRINTS; PR00846; GLHYDRLASE56.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|PIRSR:PIRSR038193-3};
KW   Glycosidase {ECO:0000256|RuleBase:RU610713};
KW   Hydrolase {ECO:0000256|RuleBase:RU610713}.
FT   ACT_SITE    108    108       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR038193-1}.
FT   CARBOHYD    331    331       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000256|PIRSR:PIRSR038193-2}.
FT   DISULFID     19    314       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    184    200       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    339    350       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    344    398       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:KFV46952.1}.
FT   NON_TER     403    403       {ECO:0000313|EMBL:KFV46952.1}.
SQ   SEQUENCE   403 AA;  46335 MW;  9E1DA18A5766E565 CRC64;
     PLVSNSPFLS IWNAPTELCT ERTGVQLDMK FFSLIGSTLK TSIGQNITLF YPDRLGYYPY
     KNEVTGEAFN GGLPQLSLLE NHLKKAKEDI QFYIPSDEQF GLAVIDWENW RPVWIRNWGS
     KDIYRQESIE LGQQRDLSLS EAEARTIAKM EFEAAAKSIM LESLKLGIKM KPNRLWGYYL
     YPDCYNYDYK QNPHNYTGTC LDIEIERNNE LNWLWEKSTA LYPSVYLETA LRSSRNAQLF
     VRNRVQEAIR ISYVSNSTHP LPVFVYTRPV FTDVYEEYLS QDDLVNTIGE SAALGASGIV
     IWGDMNLTQN KNTCRTLDNY LRTTLTPYLI NVTMAARICS QVLCQDSGAC ARKKWNSSDY
     LHLNPENIVI QMTKDGKYTL QGQPAFQDLQ TFIENFDCHC YAG
//
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