ID A0A091NI01_9PASS Unreviewed; 390 AA.
AC A0A091NI01;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
DE Flags: Fragment;
GN ORFNames=N310_09191 {ECO:0000313|EMBL:KFP78535.1};
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:KFP78535.1, ECO:0000313|Proteomes:UP000053537};
RN [1] {ECO:0000313|EMBL:KFP78535.1, ECO:0000313|Proteomes:UP000053537}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N310 {ECO:0000313|EMBL:KFP78535.1};
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-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|RuleBase:RU610713}.
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DR EMBL; KK833811; KFP78535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091NI01; -.
DR Proteomes; UP000053537; Unassembled WGS sequence.
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; 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 PRINTS; PR00848; SPERMPH20.
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:UP000053537}.
FT ACT_SITE 108
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT DISULFID 19..301
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 171..187
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 326..337
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 331..385
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFP78535.1"
FT NON_TER 390
FT /evidence="ECO:0000313|EMBL:KFP78535.1"
SQ SEQUENCE 390 AA; 45220 MW; 1C5F5C4F7DCAFBB6 CRC64;
PLVSNLPFLS IWNAPTELCT ERTGVHLDMN FFPLIGSTLK TSVGQNITLF YPDRLGYYPY
KNEVTGEEFN GGFPQLSLLE NHLKKAKEDI QFYIPSDEQF GLAVIDWENW RPVWIRNWGS
KDIYRQQYTE ARIIAKMEFE AAAKSFMLET LKLGIEMKPN RLWGYYLYPD CYNYDYKQNP
YNYTGTCLDI EIQRNNELNW LWEKSTALYP SIYLETALRS SRNAQLFVRN RVQEAIRISY
VSNSTHPLPV FVYTRPVFTD VYDEYLSEDD LVNTIGESAA LGASGIVIWG DMNLTQNKNT
CRTLDNYLRR TLTPYLINIT MASRICSQVL CQDSGACARK KWNSGDYLHL NPENIVIQIT
KDGKYTLQGQ PSFQDLQTFI DKFDCHCYAG
//
