ID   EGLC_ASPOR              Reviewed;         463 AA.
AC   Q2UUZ1;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=Probable glucan endo-1,3-beta-glucosidase eglC;
DE            EC=3.2.1.39;
DE   AltName: Full=Endo-1,3-beta-glucanase eglC;
DE   AltName: Full=Laminarinase eglC;
DE   Flags: Precursor;
GN   Name=eglC; ORFNames=AO090009000117;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- FUNCTION: Glucanases play a role in cell expansion during growth, in
CC       cell-cell fusion during mating, and in spore release during
CC       sporulation. This enzyme may be involved in beta-glucan degradation and
CC       also function biosynthetically as a transglycosylase (By similarity).
CC       {ECO:0000250}.
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;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-
CC       anchor {ECO:0000250}. Secreted, cell wall {ECO:0000250}.
CC       Note=Covalently-linked GPI-modified cell wall protein. {ECO:0000250}.
CC   -!- PTM: The GPI-anchor is attached to the protein in the endoplasmic
CC       reticulum and serves to target the protein to the cell surface. There,
CC       the glucosamine-inositol phospholipid moiety is cleaved off and the
CC       GPI-modified mannoprotein is covalently attached via its lipidless GPI
CC       glycan remnant to the 1,6-beta-glucan of the outer cell wall layer (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 17 family. {ECO:0000305}.
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DR   EMBL; AP007150; BAE54624.1; -; Genomic_DNA.
DR   RefSeq; XP_001816626.1; XM_001816574.2.
DR   AlphaFoldDB; Q2UUZ1; -.
DR   SMR; Q2UUZ1; -.
DR   STRING; 510516.Q2UUZ1; -.
DR   CAZy; GH17; Glycoside Hydrolase Family 17.
DR   GlyCosmos; Q2UUZ1; 3 sites, No reported glycans.
DR   EnsemblFungi; BAE54624; BAE54624; AO090009000117.
DR   GeneID; 5988556; -.
DR   KEGG; aor:AO090009000117; -.
DR   VEuPathDB; FungiDB:AO090009000117; -.
DR   HOGENOM; CLU_028820_1_1_1; -.
DR   OMA; WDDVGCP; -.
DR   OrthoDB; 1110018at2759; -.
DR   Proteomes; UP000006564; Chromosome 1.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR000490; Glyco_hydro_17.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR16631; GLUCAN 1,3-BETA-GLUCOSIDASE; 1.
DR   PANTHER; PTHR16631:SF13; GLUCAN ENDO-1,3-BETA-GLUCOSIDASE EGLC-RELATED; 1.
DR   Pfam; PF00332; Glyco_hydro_17; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cell membrane; Cell wall;
KW   Cell wall biogenesis/degradation; Glycoprotein; GPI-anchor; Hydrolase;
KW   Lipoprotein; Membrane; Polysaccharide degradation; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..440
FT                   /note="Probable glucan endo-1,3-beta-glucosidase eglC"
FT                   /id="PRO_0000395145"
FT   PROPEP          441..463
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000395146"
FT   REGION          317..354
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          396..430
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        128
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   ACT_SITE        239
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O22317"
FT   LIPID           440
FT                   /note="GPI-anchor amidated glycine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        183
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        312
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   463 AA;  46656 MW;  0D6C9932A360FDA8 CRC64;
     MQLTHLLAFA LSLATSEAAY KGFNYGATKS DGSVKSQSDF ESEFSTAKNL VGTSGFTSAR
     LYTMIQGGTT NSPISAIPAA IAENTSLLLG LWASGGGMDN ELAALKSAIS QYGDSFAKLV
     VGISVGSEDL YRASSEGEKV NAGIGIGPDD LVSFIKEVRS IISGTALSSV PIGHVDTWTA
     WTNGSNSAVI DAVDWLGFDG YPYFQSSMSN SISDAKSLFD DSVAKTKAVA KGKEVWITET
     GWPVSGSTQN LGVASLANAK TYWDEVGCPL FDETNTWWYI LQDANPTTPN PSFGVVGSTL
     STTPLFDLSC SNSTRPSASA SSSAAGSATP VGSAVPSGSA AVNPSSSGIV SSAVPSTTPG
     FTVGKGFRPS NSSAAAYYSS ASASGSAYPK FTKTASGSSA TSTTAGSSSD SSSTNSGKSS
     SESSSTNSGA SASSSILATG GASSVSGSVF GALVAVFAFV ATL
//