EBDG_HYPVI
ID EBDG_HYPVI Reviewed; 890 AA.
AC C0LRA7;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 25-MAY-2022, entry version 46.
DE RecName: Full=Exo-beta-D-glucosaminidase {ECO:0000312|EMBL:ACN62417.1};
DE EC=3.2.1.165;
DE Flags: Precursor;
GN Name=gls1 {ECO:0000312|EMBL:ACN62417.1};
OS Hypocrea virens (Gliocladium virens) (Trichoderma virens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=29875;
RN [1] {ECO:0000312|EMBL:ACN62417.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Abdul Murad A.M., Badrun R., Yang Ahmad Z., Khairuddin F., Mohd Adnan A.,
RA Ahmad Zairun M., Kamaruddin S., Priyatno T.P., Quay D.H.X., Zainal Z.,
RA Mahadi N.M., Hassan O., Abu Bakar F.D.;
RT "Expressed sequence tags from Trichoderma virens reveal genes encoding for
RT chitin modifying enzymes.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Hydrolyzes chitosan and chitooligosaccharides with retention
CC of anomeric configuration. Has no activity against beta-D-galactoside,
CC beta-D-glucuronide, beta-D-mannoside, chitin, glycol chitosan,
CC cellulose, N,N'-diacetylchitibiose and pNP-GlcNAc (By similarity).
CC {ECO:0000250|UniProtKB:Q4R1C4}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of chitosan or chitosan oligosaccharides to remove
CC successive D-glucosamine residues from the non-reducing termini.;
CC EC=3.2.1.165; Evidence={ECO:0000250|UniProtKB:Q4R1C4};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q4R1C4}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000250|UniProtKB:Q4R1C4}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000255}.
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DR EMBL; FJ754260; ACN62417.1; -; mRNA.
DR AlphaFoldDB; C0LRA7; -.
DR SMR; C0LRA7; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0052761; F:exo-1,4-beta-D-glucosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; ISS:UniProtKB.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; ISS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR043534; EBDG/EBM.
DR InterPro; IPR028829; Exo-b-D-glucosamin.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR041351; Ig_GlcNase.
DR InterPro; IPR041447; Mannosidase_ig.
DR PANTHER; PTHR43536; PTHR43536; 1.
DR PANTHER; PTHR43536:SF1; PTHR43536:SF1; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF18368; Ig_GlcNase; 1.
DR Pfam; PF17786; Mannosidase_ig; 1.
DR SUPFAM; SSF49303; SSF49303; 3.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Chitin degradation; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..26
FT /evidence="ECO:0000250|UniProtKB:Q56F26"
FT /id="PRO_0000399049"
FT CHAIN 27..890
FT /note="Exo-beta-D-glucosaminidase"
FT /evidence="ECO:0000250|UniProtKB:Q56F26, ECO:0000255"
FT /id="PRO_0000399050"
FT ACT_SITE 462
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q56F26"
FT ACT_SITE 537
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q56F26"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 576
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 687
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 890 AA; 98811 MW; CA246878D8B1813A CRC64;
MIAKAVAALL LGSGLASAAG TPLTSKAGDK VPIPDWDLKS SSEVSKDLKG LSKPGVDTSA
WYHAGTSKCT LMACLLNAGI YKDEDLWYSD NLNHFNWGQF SIPWLYRHEF ALAPAKGKHF
ILQTNGITSK ADLFFNGQQI ADSEYQAGAY AGRTYDITSL AAKDNAFVVQ VHPTDYLYDF
ALGYVDWNPY PPDNGTGIWR DITVKETGSV SMGPISVVVD IDVPVESSPA KVTIRAEAQN
LENVAVVLDA EAVVSGNSCS GGPLKQTVKL APGEKKLVEF TKTIAKPKIW WPKQWGDQPL
YNAKVTFSVN KAVSDTAQTN FGVRKVTSFV NQYNDTQYSV NGHPFQVVGG GYGADMFLRW
DGDRFTRIVE YMLDMHQNTI RLEGKMEHPE LYEICDKYGL MVMPGWECCD KWEAWAYNDE
LAIFPPPVWD DNDYQTANYS MIHEASMLQP HPSVLTFLVG SDFWPNDEAV VLYVNALKNA
GWQTPIIASA SKRGFPALLG PGGMKMDGPY DWVPPNYWYD TEPSEDRLGA AFGFGSELGA
GVGTPELGSL KRFLSQSDLN DLWKNPNKNL YHMSTNVSSF YNRKIYNQGL FKRYGAPTSL
DDYLLKAQMM DYEATRAQYE GFSSLWTASR PATGNIYWML NNAWPSLHWN QFGYYMHPAG
SYFGTKVGSR IEHVAYNYQK KEVWVINHSL DQTGPRKVDI ELIDTNGKQI AKQSVNINTK
ANSGFKAADI SSQIGKLSSV AFLRLILSDS KGNVLSRNVY WVTNSIDKLD WDSSTWYYTQ
VTSFVDYTPL NKLSAAQISV TTGSSRRVAG VPGTQTRTVT LENKPSVPAV FIRLTLVDKS
GNDVNPVSWT DNYVTLWPKE KLQLEVGGWD ASGDSIQVSG RNIAATTVKL
