ID G5BZQ1_HETGA Unreviewed; 481 AA.
AC G5BZQ1;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
DE Flags: Fragment;
GN ORFNames=GW7_10448 {ECO:0000313|EMBL:EHB14762.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB14762.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB14762.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
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; JH172612; EHB14762.1; -; Genomic_DNA.
DR AlphaFoldDB; G5BZQ1; -.
DR STRING; 10181.G5BZQ1; -.
DR eggNOG; ENOG502QTUU; Eukaryota.
DR InParanoid; G5BZQ1; -.
DR Proteomes; UP000006813; 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:SF7; HYALURONIDASE-4; 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:UP000006813}.
FT ACT_SITE 147
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT CARBOHYD 368
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT DISULFID 59..351
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 223..237
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 376..387
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 381..435
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 437..446
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EHB14762.1"
SQ SEQUENCE 481 AA; 55023 MW; 025E82BCC3D0DF3C CRC64;
MKLSPEGQFR LCIIQSIHLT SWLLIFLNLN SVCSLKPAQL PMYQRKPFIA AWNTPTDQCL
KKYNVTLNLQ MFQVTGSTLS KARGQNVTIF YPNRLGYYPW YTSHGVPING GLPQNISLEV
HLKKAGQDID YYIPAKDFSG LAIIDWEYWR PQWTRNWNAK DVYRRKSKEL ISDMQRNVKS
TDIEYLAKAT FEESAKEFMM KTIKLGIKKR PKGLWGYYLY PDCHNYNMNE PNYTGSCPEE
AVLKNNELSW LWNSSAALYP SIAIKKSFRD HETVLHFSKF RVQESMRIST MTSHEYALPV
FVYTRLGYRD DPLFFLSRQD LINTIGESAA LGAAGIVIWG DMNLTSSEEN CTKVNQFLSS
DFGSYIVNMS TAAEVCSLYL CRNNGRCIRK TWNASDYLYL NNESYHIEIS EDGEFSVKGN
VTDADLAMMK EKFFCHCYQG YEGADCREIK EADGSAGLSS CSGSPMTLCL LSLASYQNIQ
V
//