EGLC_ASPFU
ID EGLC_ASPFU Reviewed; 446 AA.
AC Q4WG16;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=AFUA_3G00270;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(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; AAHF01000010; EAL86311.1; -; Genomic_DNA.
DR RefSeq; XP_748349.1; XM_743256.1.
DR AlphaFoldDB; Q4WG16; -.
DR SMR; Q4WG16; -.
DR STRING; 746128.CADAFUBP00004720; -.
DR CAZy; GH17; Glycoside Hydrolase Family 17.
DR EnsemblFungi; EAL86311; EAL86311; AFUA_3G00270.
DR GeneID; 3506119; -.
DR KEGG; afm:AFUA_3G00270; -.
DR VEuPathDB; FungiDB:Afu3g00270; -.
DR eggNOG; ENOG502SI3D; Eukaryota.
DR HOGENOM; CLU_028820_0_2_1; -.
DR InParanoid; Q4WG16; -.
DR OMA; TNTWWYI; -.
DR OrthoDB; 966331at2759; -.
DR Proteomes; UP000002530; Chromosome 3.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042124; F:1,3-beta-glucanosyltransferase activity; IBA:GO_Central.
DR GO; GO:0042973; F:glucan endo-1,3-beta-D-glucosidase activity; IBA:GO_Central.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:AspGD.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IDA:AspGD.
DR GO; GO:0005975; P:carbohydrate metabolic process; IDA:AspGD.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR000490; Glyco_hydro_17.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00332; Glyco_hydro_17; 1.
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..423
FT /note="Probable glucan endo-1,3-beta-glucosidase eglC"
FT /id="PRO_0000395142"
FT PROPEP 424..446
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000395143"
FT REGION 393..416
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 423
FT /note="GPI-anchor amidated asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 370
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 446 AA; 44651 MW; BC92A444453E63B3 CRC64;
MQFTHLVALA LALATSEAAH QGFNYGNTKS DGSAKSQADF QAEFSTAKNL VGTSGFTSAR
LYTMIQGGTA NTPISAIPAA ITEQTSLLLG LWASGGNFAN EIAALKAAIA QYGDDLAKLV
VGISVGSEDL YRNSVDGVKA NAGIGTNPDE IVSYINEVRS TIAGTKLSGA PIGHVDTWTA
WVNGSNSAVI DACDWLGFDG YPYFQNTMAN SISDAKALFD ESVAKTQAVA KGKEVWITET
GWPVSGKTEN LAVANLANAK TYWDEVGCPL FGKTNTWWYI LQDADPVTPN PSFGIVGSTL
STTPLFDLSC SASSSSSAAA AASSTAGPSA SSVIGGKASG FTTAAANSAK PTFTVGKGPG
GSYNGTGFWN STSSARPSSS AISGSSSGSA AGSSGAGASG ASGQSSSSTG SSSAPSTSNI
LSNAASGLSG SIFGAVVAVC LALAAL
