EGLC_ASPOR
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 25-MAY-2022, entry version 76.
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 EnsemblFungi; BAE54624; BAE54624; AO090009000117.
DR GeneID; 5988556; -.
DR KEGG; aor:AO090009000117; -.
DR VEuPathDB; FungiDB:AO090009000117; -.
DR HOGENOM; CLU_028820_1_1_1; -.
DR OMA; TNTWWYI; -.
DR Proteomes; UP000006564; Chromosome 1.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 InterPro; IPR017853; Glycoside_hydrolase_SF.
DR SUPFAM; SSF51445; SSF51445; 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
