EXGD_ASPNC
ID EXGD_ASPNC Reviewed; 830 AA.
AC A2QX52;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=An11g07660;
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: 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM270244; CAK45960.1; -; Genomic_DNA.
DR RefSeq; XP_001394735.1; XM_001394698.1.
DR AlphaFoldDB; A2QX52; -.
DR SMR; A2QX52; -.
DR CAZy; GH5; Glycoside Hydrolase Family 5.
DR PaxDb; A2QX52; -.
DR PRIDE; A2QX52; -.
DR EnsemblFungi; CAK45960; CAK45960; An11g07660.
DR GeneID; 4984985; -.
DR KEGG; ang:ANI_1_2268094; -.
DR VEuPathDB; FungiDB:An11g07660; -.
DR HOGENOM; CLU_004624_4_0_1; -.
DR Proteomes; UP000006706; Chromosome 7R.
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 Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..830
FT /note="Probable glucan 1,3-beta-glucosidase D"
FT /id="PRO_0000395165"
FT TOPO_DOM 1..307
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 329..830
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 260..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..91
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 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
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 397
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 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 830 AA; 93303 MW; E07B09114631E566 CRC64;
MPGHSRSRDR LSPSSELDDA DPVYSPSVYQ REHYYNNDSL FDSADDDYTR TPRNVYSYET
HDEYHDDDDD DDDVHEHDHD HEYDDKFEEP WVPLRAQVEG DQWREGFETA IPKEEDVTQA
KEYQYQMSGA LGDDGPPPLP SDALGRGKGK KRLDRETRRQ RRKERLAAFF KHKNGSASAG
LVSGDALAKL LGSQDGDEDC LSHLGTERAD SMSQKNLEGG RQRKLPVLSE EPMMLRPFPA
VAPTGQTQGR VVSGAQLEEG GPGMEMRHRG GGGPPAEGLL QKEGDWDGST KGSSTSARPS
FWKRYHKTFI FFAILIVLAA IAIPVGIIEA RRLHGTSGGD NSSNSNLKGI SRDSIPAYAR
GTYLDPFTWY DTTDFNVTFT NATVGGLSIM GLNSTWNDSA QANENVPPLN EKFPYGSQPI
RGVNLGGWLS IEPFIVPSLF DTYTSSEGII DEWTLSEKLG DSAASVIEKH YATFITEQDF
ADIRDAGLDH VRIQFSYWAI KTYDGDPYVP KIAWRYLLRA IEYCRKYGLR VNLDPHGIPG
SQNGWNHSGR QGTIGWLNGT DGELNRQRSL EMHDQLSQFF AQDRYKNVVT IYGLVNEPLM
LSLPVEKVLN WTTEATNLVQ KNGIKAWVTV HDGFLNLDKW DKMLKTRPSN MMLDTHQYTV
FNTGEIVLNH TRRVELICES WYSMIQQINI TSTGWGPTIC GEWSQADTDC AQYVNNVGRG
TRWEGTFSLT DSTQYCPTAS EGTCSCTQAN AVPGVYSEGY KTFLQTYAEA QMSAFESAMG
WFYWTWATES AAQWSYRTAW KNGYMPKKAY SPSFKCGDTI PSFGNLPEYY
