EXGA_ASPCL
ID EXGA_ASPCL Reviewed; 415 AA.
AC A1CRV0;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 25-MAY-2022, entry version 72.
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=ACLA_031040;
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1;
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAW08371.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DS027059; EAW08371.1; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001269797.1; XM_001269796.1.
DR AlphaFoldDB; A1CRV0; -.
DR SMR; A1CRV0; -.
DR STRING; 5057.CADACLAP00002273; -.
DR PRIDE; A1CRV0; -.
DR GeneID; 4700820; -.
DR KEGG; act:ACLA_031040; -.
DR eggNOG; ENOG502QPYU; Eukaryota.
DR OrthoDB; 896412at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
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 Glycosidase; Hydrolase; Manganese; Metal-binding;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..415
FT /note="Probable glucan 1,3-beta-glucosidase A"
FT /id="PRO_0000393527"
FT REGION 335..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 210
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 307
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT DISULFID 290..414
FT /evidence="ECO:0000250"
FT DISULFID 315..341
FT /evidence="ECO:0000250"
SQ SEQUENCE 415 AA; 45665 MW; 86978A724C6C1B67 CRC64;
MLSRLSQTAL VALSLMTVLT EAVPSRMRIQ TRDSVNYQSE IVRGVNLGGW LVLEPWITPS
IFENGGGAAV DEWTLAEVLG KDKARAILSQ HWSSFITQDD FNQIAQAGMN HVRIPVGYWA
VSAPDEPYVD GQLEFLDNAI SWARAAGLKV MIDLHGAPGS QNGFDNSGRK GPIAWQQGDT
VARTVDAFKA LAERYLPESD VVTAIEAVNE PNIPGGVNEG QLKEYYNQVL EVVHSINPDA
GVFLSDGFLA TASWNGYANG ENVVMDTHHY HMFDNTLISL DINAHVRAAC EFGNQIKGSD
KPVVVGEWTG ALTDCTKHLN GKDIPTRYEG QWANSPRYGD CGNKRQGSSS GLSEQERSDT
RRFIEAQLDA YEGKNGWLFW TWKTEGAPGW DMQDLLANGL FPNPPTERQY GNQCA
