EXGD_ASPFC
ID EXGD_ASPFC Reviewed; 833 AA.
AC B0Y7W2;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Probable glucan 1,3-beta-glucosidase D;
DE EC=3.2.1.58;
DE AltName: Full=Exo-1,3-beta-glucanase D;
GN Name=exgD; ORFNames=AFUB_075220;
OS Neosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus
OS fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=451804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CEA10 / CBS 144.89 / FGSC A1163;
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: Glucosidase involved in the degradation of cellulosic
CC biomass. Active on lichenan (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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC {ECO:0000305}.
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DR EMBL; DS499599; EDP49493.1; -; Genomic_DNA.
DR AlphaFoldDB; B0Y7W2; -.
DR SMR; B0Y7W2; -.
DR EnsemblFungi; EDP49493; EDP49493; AFUB_075220.
DR VEuPathDB; FungiDB:AFUB_075220; -.
DR HOGENOM; CLU_004624_4_0_1; -.
DR PhylomeDB; B0Y7W2; -.
DR Proteomes; UP000001699; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004338; F:glucan exo-1,3-beta-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; 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 membrane; Cell wall biogenesis/degradation;
KW Glycoprotein; Glycosidase; Hydrolase; Membrane; Polysaccharide degradation;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..833
FT /note="Probable glucan 1,3-beta-glucosidase D"
FT /id="PRO_0000395162"
FT TOPO_DOM 1..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..833
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 599
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 704
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 383
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 671
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 691
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 833 AA; 94775 MW; 6A08231B6A8A1855 CRC64;
MPTHSRSRDR YGGRDSDREA RYDYDYARRR YATDDDDDYD DDELEHDLTE RRYRRDGYRP
PRESRARGYY ERDAEGAADE ELLGNERDPG PRASRSYGDD YDARRREHSR AREAPRRSER
HRDRDREGRS RRRAYEDDGR HRTRDGRRDR GRESDGEARR SRRREAGRET AARKHRSSDS
TNSASHLLSA DALAKLGAQY EKEERRKREI AKDAAKAERK RQKKLAVVGE ETRALRDPPG
ESHRDRTKAR VASGAYLEEG RSPEMRVRHR GGGGPAMEAR WRKEGSWGGT MDDSGGGRPF
WKRKRWIGLG ALIIILVIVI PVAVVVSKKH DNKSDPADSQ GTSPGKSNLD GLSHDSIPAY
AQGTYLDPWT WYDTTDFNVT FTNETVGGLS IMGLNSTWDD SARPNDNVPP LNEPFPYGSQ
PIRGVNLGGW LSIEPFIVPS LFDSYSSVSG IIDEWTLSKR LGSSAASTLE KHYATFITEQ
DFADIRDAGL DHVRIQYSYW AVATYDDDPY VAKISWRYLL RAIEYCRKYG LRVNLDPHGI
PGSQNGWNHS GREGVIGWLN GTDGELNRNR SLAVHDSVSK FFAQDRYKNI VTIYGLVNEP
LMLSLSIEDV LDWTTEATKL VQKNGITAYV ALHDGFLNLS KWKSMLKNRP DKMLLDTHQY
TIFNTGQIGL NHTAKVNLIC NDWYNMIKEI NSTSTGWGPT ICGEWSQADT DCAKYLNNVG
RGTRWEGTFS LTDSTQYCPT ADTGPPCSCA NANADVSKYS ADYKKFLQTY AEAQMSAFET
GQGWFYWTWR TESAAQWSYR TAWKNGFMPA KAYAPSFRCG DAVPDFGDLP EYY
