ID M7B9S8_CHEMY Unreviewed; 464 AA.
AC M7B9S8;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Hyaluronidase {ECO:0000256|RuleBase:RU610713};
DE EC=3.2.1.35 {ECO:0000256|RuleBase:RU610713};
GN ORFNames=UY3_08988 {ECO:0000313|EMBL:EMP33904.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP33904.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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 EMBL; KB535020; EMP33904.1; -; Genomic_DNA.
DR RefSeq; XP_007061937.1; XM_007061875.1.
DR AlphaFoldDB; M7B9S8; -.
DR STRING; 8469.M7B9S8; -.
DR GeneID; 102946634; -.
DR KEGG; cmy:102946634; -.
DR eggNOG; ENOG502QTUU; Eukaryota.
DR OrthoDB; 5344684at2759; -.
DR Proteomes; UP000031443; Unassembled WGS sequence.
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; IPR000742; EGF-like_dom.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR018155; Hyaluronidase.
DR PANTHER; PTHR11769; HYALURONIDASE; 1.
DR PANTHER; PTHR11769:SF38; HYALURONIDASE; 1.
DR Pfam; PF01630; Glyco_hydro_56; 1.
DR PIRSF; PIRSF038193; Hyaluronidase; 1.
DR PRINTS; PR00846; GLHYDRLASE56.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS01186; EGF_2; 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:UP000031443};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..464
FT /note="Hyaluronidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004079819"
FT DOMAIN 424..435
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS01186"
FT ACT_SITE 132
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-1"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-2"
FT DISULFID 41..337
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 208..224
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 362..373
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 367..424
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
FT DISULFID 426..435
FT /evidence="ECO:0000256|PIRSR:PIRSR038193-3"
SQ SEQUENCE 464 AA; 53006 MW; 9ACE4426AD56A0A1 CRC64;
MLLLLLLCPE LPRGHNLKPS LPPIVPDRPF LVAWNAPTAR CWTSYEVPLS VASFSLLVNA
QEDFTGGNVT IFYYDQLGLY PYYLNTTTPP VAVNGGCPQN ASLLDHLDKM ASDIAATMPS
ASFAGLSVID WENWRPQWIR NWDKKNVYRA MSAQLVRQRN PRWPDEQVEL EAKWEFETAA
ARFMVETLKL AQLLRPGGWW GYYLFPECYN YHYWDDFENF TGGCPQVEVQ RNNKLLWLWE
QSKALYPSIY MEEVLRASPQ GKKFVQAKLS EALRVAQLPS ANHSLPVFAY ARPFYSYTLK
ELTQTDLVYT IGQAAAMGAH GIVLWGGVEY SRNQPNCVKI QKYLTGTLGP YIINVTTATK
LCSQFVCNNH GRCLRRKMDS DSYLHLDASS FQIRVDTATH GPHVSVKGAL TTLQRDRMKQ
EFTCHCYQGW SGEHCHSRGQ SNRLWAWDLC IPMVVMSAIW TWGM
//
