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Database: UniProt
Entry: A0A091N6Q4_9PASS
LinkDB: A0A091N6Q4_9PASS
Original site: A0A091N6Q4_9PASS 
ID   A0A091N6Q4_9PASS        Unreviewed;       409 AA.
AC   A0A091N6Q4;
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=N310_03624 {ECO:0000313|EMBL:KFP85523.1};
OS   Acanthisitta chloris (rifleman).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Acanthisittidae;
OC   Acanthisitta.
OX   NCBI_TaxID=57068 {ECO:0000313|EMBL:KFP85523.1};
RN   [1] {ECO:0000313|EMBL:KFP85523.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP85523.1};
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; KK843492; KFP85523.1; -; 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    118    118       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR038193-1}.
FT   CARBOHYD    330    330       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000256|PIRSR:PIRSR038193-2}.
FT   DISULFID     30    313       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    187    201       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    338    349       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    343    397       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   DISULFID    399    408       {ECO:0000256|PIRSR:PIRSR038193-3}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:KFP85523.1}.
FT   NON_TER     409    409       {ECO:0000313|EMBL:KFP85523.1}.
SQ   SEQUENCE   409 AA;  45910 MW;  3169B6D99A6FDD92 CRC64;
     LPAPAHTGGP GPVLVNRPFV TVWNIPTERC ATKYNVTLNL EVFDVLANDQ QSFAGQDITL
     FYSDELGLFP YYTSEGLPVN GGLPQNASLE THLHKATQDI KVTLPSPAYS GLAVIDWENN
     WDTMQIYQQK SEELVQQQHP EWPPKKVNET AKLQFEESAC NFMNKTLWLG KSLRSNAYWG
     FYGFPSCYNN DFDSQSYNGT CPEVEQQRNK NLSWLWSSSQ ALYPSIYLPS RLNGTNKVLA
     YVRHRVAEAF AVQHGILDNG ISVLPYSQIA FERTVDFLSQ EDLMNTIGES AAQGAAGIIL
     WGSLDYSSSK EMCLRLKDYV EGPLGHYVVN VTASADLCSQ TLCSGRGRCV RQENKQSYLH
     LDPFRFAIDL HAGKPWLVAQ SLESGDDTSR LAKEFSCQCY DKWQGPHCD
//
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