ID EXGD_ASPFN Reviewed; 831 AA.
AC B8NNK9;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 76.
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=AFLA_129100;
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC 167;
RX PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963481; EED48687.1; -; Genomic_DNA.
DR RefSeq; XP_002382103.1; XM_002382062.1.
DR AlphaFoldDB; B8NNK9; -.
DR SMR; B8NNK9; -.
DR STRING; 332952.B8NNK9; -.
DR GlyCosmos; B8NNK9; 11 sites, No reported glycans.
DR EnsemblFungi; EED48687; EED48687; AFLA_129100.
DR VEuPathDB; FungiDB:AFLA_012738; -.
DR eggNOG; ENOG502QRG8; Eukaryota.
DR HOGENOM; CLU_004624_4_0_1; -.
DR OMA; WWYWTWK; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
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 Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR001547; Glyco_hydro_5.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR31297:SF22; GLUCAN 1,3-BETA-GLUCOSIDASE 2; 1.
DR PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR Pfam; PF00150; Cellulase; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 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..831
FT /note="Probable glucan 1,3-beta-glucosidase D"
FT /id="PRO_0000395163"
FT TOPO_DOM 1..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..831
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..62
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..157
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 597
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 702
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 442
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 546
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 558
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 610
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 636
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 669
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 831 AA; 95079 MW; 9898B3C61F07541B CRC64;
MPSHSRSRDR YRGERDPSRR YREVYDDDDD DDFDYHPRER RRYRRDDYQH DIRSHESPNY
NDDLNEYDAA AEDPAVPLRS HDVEGRRRER SRAGESPIAS PSRRDRNRGG EEYRRHGTYG
DGGSPTRAMR DRRHRSRDGQ RARPRDMDRE ARRQRRRERA RGAAAMKHKS SDSTNSGSHL
LSADALAKLR SHYDEEDQRE RSQEQEQPRL ESKRQRKRPI VGDEPQALAP FPDETPRGQS
KGRIVSGAYL EEGHPEMEVR HRGGGGPAME ARWRKEGNWD GTMEGSDAQP PFWKRKKWWI
VIGVLVVVLA IVIPVAVVMS KKHGHDDDKS GSSSSVDNSD SPYISSLDGL SHDSIPESAQ
GSILDPWTWY DTRDFNLTFT NETVGGLPIM GLNSTWDDST RPNDNVPPLN ESFPYGSQPI
RGVNLGGWLS IEPFIVPSLF ENYSSKDRII DEYTLCKKLG SSAASTIEKH YADFISEQDF
IDMRDAGLDH VRIQFSYWAV TTYDDDPYVA KISWRYLLRA IEYCRKYGLR VNLDPHGIPG
SQNGWNHSGR EGVIGWLNGT DGQLNRQRSL DFHNQISQFF AQPRYKNVVT IYGLVNEPLM
LSLPVEDVLN WTTDATKLVQ KNGISAYVTV HDGFLNLSKW KQMLKDRPDR MFLDTHQYTI
FNTGQIVLNH TDRVKLICND WYNMIKEINT TSAGWGPTIC GEWSQADTDC AQYLNNVGRG
TRWEGTFAIG DSTVYCPTAD TGPTCSCASA NAPPADYSDG YKKFLQTYAE AQMSAFGTAQ
GWFYWTWHTE SAAQWSYKTA WKNGYMPKKA YAPDFKCGDD IPSFGDLPEY Y
//
