GUX2_HYPJR
ID GUX2_HYPJR Reviewed; 471 AA.
AC A0A024SH76;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 1.
DT 25-MAY-2022, entry version 30.
DE RecName: Full=Exoglucanase 2;
DE EC=3.2.1.91 {ECO:0000250|UniProtKB:P07987};
DE AltName: Full=1,4-beta-cellobiohydrolase;
DE AltName: Full=Cellobiohydrolase 6A;
DE Short=Cel6A;
DE AltName: Full=Exocellobiohydrolase II;
DE Short=CBHII;
DE AltName: Full=Exoglucanase II;
DE Flags: Precursor;
GN Name=cbh2; ORFNames=M419DRAFT_122470;
OS Hypocrea jecorina (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30)
OS (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=1344414;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX DOI=10.1089/ind.2013.0015;
RA Koike H., Aerts A., LaButti K., Grigoriev I.V., Baker S.E.;
RT "Comparative genomics analysis of Trichoderma reesei strains.";
RL Ind. Biotechnol. 9:352-367(2013).
RN [2]
RP GLYCOSYLATION AT ASN-313 AND ASN-334.
RC STRAIN=ATCC 56765 / BCRC 32924 / NRRL 11460 / Rut C-30;
RX PubMed=12499406; DOI=10.1093/glycob/cwf089;
RA Hui J.P., White T.C., Thibault P.;
RT "Identification of glycan structure and glycosylation sites in
RT cellobiohydrolase II and endoglucanases I and II from Trichoderma reesei.";
RL Glycobiology 12:837-849(2002).
CC -!- FUNCTION: Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of
CC 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide
CC cellobiose. The degradation of cellulose involves an interplay between
CC different cellulolytic enzymes. Hydrolysis starts with endoglucanases
CC (EGs), which cut internal beta-1,4-glucosidic bonds in cellulose to
CC reduce the polymerization degree of the substrate and create new chain
CC ends for exocellobiohydrolases (CBHs). The CBHs release the
CC disaccharide cellobiose from the non-reducing end of the cellulose
CC polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose
CC and other short cello-oligosaccharides into glucose units.
CC {ECO:0000250|UniProtKB:P07987}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose
CC and cellotetraose, releasing cellobiose from the non-reducing ends of
CC the chains.; EC=3.2.1.91; Evidence={ECO:0000250|UniProtKB:P07987};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P07987}.
CC -!- DOMAIN: The enzyme consists of two functional domains, a catalytic core
CC joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-,
CC and proline-rich, highly glycosylated linker sequence.
CC {ECO:0000250|UniProtKB:P07987}.
CC -!- PTM: Asn-334 contains mainly a high-mannose-type glycan (Hex(7-
CC 9)GlcNAc(2)) in a 3:1 ration with a single GlcNAc. Asn-313 was
CC primarily unglycosylated with a small fraction (18%) bearing a single
CC GlcNAc at this site. {ECO:0000269|PubMed:12499406}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B) family.
CC {ECO:0000305}.
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DR EMBL; KI911141; ETS04894.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A024SH76; -.
DR SMR; A0A024SH76; -.
DR iPTMnet; A0A024SH76; -.
DR EnsemblFungi; ETS04894; ETS04894; M419DRAFT_122470.
DR KEGG; trr:M419DRAFT_122470; -.
DR HOGENOM; CLU_015488_0_0_1; -.
DR OrthoDB; 957754at2759; -.
DR Proteomes; UP000024376; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.40; -; 1.
DR InterPro; IPR016288; Beta_cellobiohydrolase.
DR InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR001524; Glyco_hydro_6_CS.
DR PANTHER; PTHR34876; PTHR34876; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF01341; Glyco_hydro_6; 1.
DR PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1.
DR PRINTS; PR00733; GLHYDRLASE6.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF51989; SSF51989; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000250|UniProtKB:P07987"
FT /id="PRO_0000441279"
FT CHAIN 25..471
FT /note="Exoglucanase 2"
FT /id="PRO_5005101780"
FT DOMAIN 26..62
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 64..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 66..106
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:P07987"
FT REGION 107..471
FT /note="Catalytic"
FT /evidence="ECO:0000250|UniProtKB:P07987"
FT ACT_SITE 245
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P07987"
FT SITE 38
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:12499406"
FT SITE 199
FT /note="Transition state stabilizer that also modulates the
FT pKa of Asp-245 and may act as a proton acceptor through a
FT water chain"
FT /evidence="ECO:0000250|UniProtKB:P07987"
FT MOD_RES 25
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000250|UniProtKB:P07987"
FT CARBOHYD 111
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P07987"
FT CARBOHYD 121
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P07987"
FT CARBOHYD 130
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000250|UniProtKB:P07987"
FT CARBOHYD 133
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000250|UniProtKB:P07987"
FT CARBOHYD 134
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000250|UniProtKB:P07987"
FT CARBOHYD 139
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000250|UniProtKB:P07987"
FT CARBOHYD 146
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P07987"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc) asparagine"
FT /evidence="ECO:0000269|PubMed:12499406"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:12499406"
FT DISULFID 200..259
FT /evidence="ECO:0000250|UniProtKB:P07987"
FT DISULFID 392..439
FT /evidence="ECO:0000250|UniProtKB:P07987"
SQ SEQUENCE 471 AA; 49653 MW; C4711BC335B1BD88 CRC64;
MIVGILTTLA TLATLAASVP LEERQACSSV WGQCGGQNWS GPTCCASGST CVYSNDYYSQ
CLPGAASSSS STRAASTTSR VSPTTSRSSS ATPPPGSTTT RVPPVGSGTA TYSGNPFVGV
TPWANAYYAS EVSSLAIPSL TGAMATAAAA VAKVPSFMWL DTLDKTPLME QTLADIRTAN
KNGGNYAGQF VVYDLPDRDC AALASNGEYS IADGGVAKYK NYIDTIRQIV VEYSDIRTLL
VIEPDSLANL VTNLGTPKCA NAQSAYLECI NYAVTQLNLP NVAMYLDAGH AGWLGWPANQ
DPAAQLFANV YKNASSPRAL RGLATNVANY NGWNITSPPS YTQGNAVYNE KLYIHAIGPL
LANHGWSNAF FITDQGRSGK QPTGQQQWGD WCNVIGTGFG IRPSANTGDS LLDSFVWVKP
GGECDGTSDS SAPRFDSHCA LPDALQPAPQ AGAWFQAYFV QLLTNANPSF L
