EBDG_HYPJE
ID EBDG_HYPJE Reviewed; 892 AA.
AC Q4R1C4;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Exo-beta-D-glucosaminidase {ECO:0000312|EMBL:BAD99604.1};
DE EC=3.2.1.165;
DE Flags: Precursor;
GN Name=gls93 {ECO:0000312|EMBL:BAD99604.1};
OS Hypocrea jecorina (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=51453;
RN [1] {ECO:0000305, ECO:0000312|EMBL:BAD99604.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 29-41; 112-135;
RP 447-461 AND 812-841, FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=PC-3-7 {ECO:0000269|PubMed:16636831};
RX PubMed=16636831; DOI=10.1007/s00253-006-0320-y;
RA Ike M., Isami K., Tanabe Y., Nogawa M., Ogasawara W., Okada H.,
RA Morikawa Y.;
RT "Cloning and heterologous expression of the exo-beta-D-glucosaminidase-
RT encoding gene (gls93) from a filamentous fungus, Trichoderma reesei PC-3-
RT 7.";
RL Appl. Microbiol. Biotechnol. 72:687-695(2006).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=16349528; DOI=10.1128/aem.64.3.890-895.1998;
RA Nogawa M., Takahashi H., Kashiwagi A., Ohshima K., Okada H., Morikawa Y.;
RT "Purification and Characterization of Exo-beta-d-Glucosaminidase from a
RT Cellulolytic Fungus, Trichoderma reesei PC-3-7.";
RL Appl. Environ. Microbiol. 64:890-895(1998).
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.
CC {ECO:0000269|PubMed:16349528, ECO:0000269|PubMed:16636831}.
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:0000269|PubMed:16349528,
CC ECO:0000269|PubMed:16636831};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 4.0. Stable between pH 6.0 and 9.0.
CC {ECO:0000269|PubMed:16349528};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius. Stable below 50 degrees
CC Celsius. {ECO:0000269|PubMed:16349528};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16349528}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space
CC {ECO:0000269|PubMed:16349528}.
CC -!- INDUCTION: By growth on GlcN or GlcNAc. {ECO:0000269|PubMed:16349528}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family. {ECO:0000255}.
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DR EMBL; AB218755; BAD99604.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4R1C4; -.
DR SMR; Q4R1C4; -.
DR CAZy; GH2; Glycoside Hydrolase Family 2.
DR CLAE; GLS2A_TRIRE; -.
DR KEGG; ag:BAD99604; -.
DR VEuPathDB; FungiDB:TrQ_000043; -.
DR OMA; VDWNPYP; -.
DR BRENDA; 3.2.1.165; 6451.
DR GO; GO:0005576; C:extracellular region; IDA: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; IDA:UniProtKB.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IDA: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 1: Evidence at protein level;
KW Carbohydrate metabolism; Chitin degradation; Direct protein sequencing;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..28
FT /evidence="ECO:0000255, ECO:0000269|PubMed:16636831"
FT /id="PRO_0000399048"
FT CHAIN 29..892
FT /note="Exo-beta-D-glucosaminidase"
FT /evidence="ECO:0000269|PubMed:16636831"
FT /id="PRO_5000052424"
FT ACT_SITE 464
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q56F26"
FT ACT_SITE 539
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q56F26"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 336
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 578
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 689
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 825
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 892 AA; 99428 MW; AA91240261C26570 CRC64;
MLANAIAALL LGSGIASAAG HGSPLTSKAG HRAVIPDWDL KSSSDVSKDL GGLSKPGVDT
SSWYHAGTSR CTIMGCLINA GVYNDEELWY SDNLNHVNWG QFSVPWVYRH EFALSPAKGK
HFLLQTNGIT SKADLFFNGK QIADKEYQSG AYAGRTYDIT NLAAKKNALL VQVYPTDYLY
DFALGYVDWN PYPSDNGSGI WRDITIKETG SVSMGPVSVL VDIDVPVEKN PARVTVRAEA
QNLESHAVEF NAAAVISGNS CSGEALKQTI KLAPGEKKLV QFTQTIKTPS IWWPKQWGDQ
PLYTAEVTFS VKGAVSDTAQ TKFGVRKVTS FVNQFNDTQY SVNGHPFQVI GGGYGADMFL
RWDSERFTRI VEYMLDMHQN TIRLEGKMEH PELYEICDEY GLMVMPGWEC CDKWEAWAYN
DELAIFPPPV WDANDYETAN YSMIHEAAMM QPHPSVLTFL VGSDFWPNDE AVVLYANALK
NAGWQTPIIA SASKRGFPAL LGPGGMKMDG PYDWVPPNYW YDVEPSEDRL GAAFGFGSEL
GAGVGTPELS SLRRFLNQSD LDDLWKNPNK NLFHMSTNAS SFYNRKIYNQ GLWKRYGAPT
SLDDYLLKAQ MMDYEATRAQ YEGFGALWTA SRPATGVIYW MLNNAWPSLH WNQFDYYLHP
AGSYFGTKVG SRIEHVAYNY QKKEIWVINH SLYQTGSRNI KVELIDMNGK QIAKKLVQVR
TKANSGFKAM DISSDINKLS SVAFLRLVLS DEKGSVLSRN VYWVTKTIDE LNWDESTWYY
TPVSKFVDYT PLNTLATAQV SVTTSGGKHL PGIPGSQTRT VTLENKSSVP AVFIRLTLVD
SKGNDVNPVS WSDNYVTLWP HEKLQLEVGG WDGSGDKIQI SGKNIKATTV KL
