ID   E13B_CRYAT              Reviewed;         270 AA.
AC   C1IE32;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 41.
DE   RecName: Full=Glucan endo-1,3-beta-glucosidase {ECO:0000305};
DE            EC=3.2.1.39 {ECO:0000269|PubMed:20079869, ECO:0000312|EMBL:ACV50413.1};
DE   AltName: Full=(1->3)-beta-glucan endohydrolase {ECO:0000305};
DE   AltName: Full=(1->3)-beta-glucanase {ECO:0000305};
DE   AltName: Full=CaLam {ECO:0000303|PubMed:20079869};
DE   AltName: Full=Endo-beta-1,3-glucanase {ECO:0000303|PubMed:20079869, ECO:0000312|EMBL:ACV50413.1};
DE   AltName: Full=Laminarinase {ECO:0000303|PubMed:20079869};
DE   Flags: Precursor;
OS   Cryptopygus antarcticus (Antarctic springtail).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Collembola;
OC   Entomobryomorpha; Isotomoidea; Isotomidae; Anurophorinae; Cryptopygus;
OC   Cryptopygus antarcticus complex.
OX   NCBI_TaxID=187623 {ECO:0000312|EMBL:ACD93221.1};
RN   [1] {ECO:0000312|EMBL:ACD93221.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND 3D-STRUCTURE
RP   MODELING.
RX   PubMed=20079869; DOI=10.1016/j.cbpb.2010.01.003;
RA   Song J.M., Nam K., Sun Y.U., Kang M.H., Kim C.G., Kwon S.T., Lee J.,
RA   Lee Y.H.;
RT   "Molecular and biochemical characterizations of a novel arthropod endo-
RT   beta-1,3-glucanase from the Antarctic springtail, Cryptopygus antarcticus,
RT   horizontally acquired from bacteria.";
RL   Comp. Biochem. Physiol. 155B:403-412(2010).
CC   -!- FUNCTION: Hydrolyzes laminarin majorily to glucose (G1), laminaribiose
CC       (L2), laminaritriose (L3), laminaritetraose (L4) and laminaripentaose
CC       (L5). Hydrolyzes laminarioligosaccharides L3, L4, L5 and
CC       laminarihexaose (L6) to G1, L2 and L3. Hardly hydrolyzes L2. Does not
CC       hydrolyze lichenan, pustulan, carboxymethyl cellulose, locust bean gum
CC       or soluble starch. {ECO:0000269|PubMed:20079869}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-
CC         beta-D-glucans.; EC=3.2.1.39; Evidence={ECO:0000269|PubMed:20079869};
CC   -!- ACTIVITY REGULATION: Ca(2+) does not affect the enzyme activity nor the
CC       thermostability. Other cations, such as Mg(2+), Mn(2+), Cu(2+), Zn(2+),
CC       Ag(+) or Hg(2+) do not cause any serious adverse effect on the
CC       activity. Also no significant change in the activity in response to the
CC       addition of 1 mM EDTA. {ECO:0000269|PubMed:20079869}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=9.98 mg/ml for 1% laminarin (at pH 6.0 and 50 degrees Celsius)
CC         {ECO:0000269|PubMed:20079869};
CC         Vmax=32.2 umol/min/mg enzyme with 1% laminarin as substrate (at pH
CC         6.0 and 50 degrees Celsius) {ECO:0000269|PubMed:20079869};
CC       pH dependence:
CC         Optimum pH is 6.0. More than 80% of its maximal activity is
CC         maintained at pH 5.5-6.5. {ECO:0000269|PubMed:20079869};
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius. Retains 20% of the maximal
CC         activity after incubation at 60 degrees Celsius for 30 min. Retains
CC         approximately 15% of the maximal activity at the temperature below 15
CC         degrees Celsius. {ECO:0000269|PubMed:20079869};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01098}.
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DR   EMBL; EU559744; ACD93221.1; -; Genomic_DNA.
DR   EMBL; FJ648734; ACV50413.1; -; mRNA.
DR   AlphaFoldDB; C1IE32; -.
DR   SMR; C1IE32; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   BRENDA; 3.2.1.39; 11159.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IDA:UniProtKB.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   1: Evidence at protein level;
KW   Glycosidase; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..270
FT                   /note="Glucan endo-1,3-beta-glucosidase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5007646702"
FT   DOMAIN          22..270
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   ACT_SITE        137
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   ACT_SITE        142
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
SQ   SEQUENCE   270 AA;  31008 MW;  70257A2C38B0B9B1 CRC64;
     MNAFTFPLLL AFCAFAHGAW VLDWEDEFNG GNLADRWNFE LGCNGWGNNE LQCYTDNRGA
     NARQEDGKLV ISAVREWWGD GVNPDKEFTS ARMTTKANWL HGKFEMRARL PKGKHLWPAF
     WMMPQNSEYG GWPRSGEIDI TEYRGQRPQQ ILGTLHFGAA PDNKGDVGTG ERDFPIDFSA
     DFHTFGLDWS PDSMQWLLDD QVYHTESLQR NFWDGVYNQN GSPFDKNFFI ILNLAVGGNF
     FGGEPFDPSE SDGWAKNTFE VEYVKKWTWN