EXGA_ASPNC
ID EXGA_ASPNC Reviewed; 416 AA.
AC A2RAR6;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Probable glucan 1,3-beta-glucosidase A;
DE EC=3.2.1.58;
DE AltName: Full=Exo-1,3-beta-glucanase 1;
DE AltName: Full=Exo-1,3-beta-glucanase A;
DE Flags: Precursor;
GN Name=exgA; Synonyms=exg1; ORFNames=An18g04100;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Beta-glucanases participate in the metabolism of beta-glucan,
CC the main structural component of the cell wall. It could also function
CC biosynthetically as a transglycosylase (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Successive hydrolysis of beta-D-glucose units from the non-
CC reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.;
CC EC=3.2.1.58;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; AM270406; CAK43212.1; -; Genomic_DNA.
DR RefSeq; XP_001398868.1; XM_001398831.2.
DR AlphaFoldDB; A2RAR6; -.
DR SMR; A2RAR6; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR PaxDb; A2RAR6; -.
DR EnsemblFungi; CAK43212; CAK43212; An18g04100.
DR GeneID; 4989974; -.
DR KEGG; ang:ANI_1_534164; -.
DR VEuPathDB; FungiDB:An18g04100; -.
DR HOGENOM; CLU_004624_0_1_1; -.
DR Proteomes; UP000006706; Chromosome 8L.
DR GO; GO:1990819; C:actin fusion focus; IEA:EnsemblFungi.
DR GO; GO:0000935; C:division septum; IEA:EnsemblFungi.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046557; F:glucan endo-1,6-beta-glucosidase activity; IEA:EnsemblFungi.
DR GO; GO:0004338; F:glucan exo-1,3-beta-glucosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070879; P:fungal-type cell wall beta-glucan metabolic process; IEA:EnsemblFungi.
DR GO; GO:1904541; P:fungal-type cell wall disassembly involved in conjugation with cellular fusion; IEA:EnsemblFungi.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cell wall biogenesis/degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Manganese; Metal-binding;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..416
FT /note="Probable glucan 1,3-beta-glucosidase A"
FT /id="PRO_5000221332"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 308
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 183
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 290..415
FT /evidence="ECO:0000250"
FT DISULFID 316..342
FT /evidence="ECO:0000250"
SQ SEQUENCE 416 AA; 45526 MW; 9FC5AADB23A03E24 CRC64;
MFVESAKKAL LALSLLAASA QAVPRVRRQG ASSSFDYKSQ IVRGVNLGGW LVTEPWITPS
LYDSTGGGAV DEWTLCQILG KDEAQAKLSS HWSSFITQSD FDRMAQAGLN HVRIPIGYWA
VAPIDGEPYV SGQIDYLDQA VTWARAAGLK VLVDLHGAPG SQNGFDNSGH RGPIQWQQGD
TVNQTMTAFD ALARRYAQSD TVTAIEAVNE PNIPGGVNED GLKNYYYGAL ADVQRLNPST
TLFMSDGFQP VESWNGFMQG SNVVMDTHHY QVFDTGLLSM SIDDHVKTAC SLATQHTMQS
DKPVVVGEWT GALTDCAKYL NGVGNAARYD GTYMSTTKYG DCTGKSTGSV ADFSADEKAN
TRRYIEAQLE AYEMKSGWLF WTWKTEGAPG WDMQDLLANQ LFPTSPTDRQ YPHQCS
