GUX2_HYPJE
ID GUX2_HYPJE Reviewed; 471 AA.
AC P07987;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 25-MAY-2022, entry version 165.
DE RecName: Full=Exoglucanase 2;
DE EC=3.2.1.91;
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;
OS Hypocrea jecorina (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=51453;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=VTT-D-80133;
RX PubMed=3596237; DOI=10.1016/0378-1119(87)90472-0;
RA Teeri T.T., Lehtovaara P., Kauppinen S., Salovuori I., Knowles J.;
RT "Homologous domains in Trichoderma reesei cellulolytic enzymes: gene
RT sequence and expression of cellobiohydrolase II.";
RL Gene 51:43-52(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26921 / CBS 392.92 / QM9414;
RX DOI=10.1038/nbt0387-274;
RA Chen C.M., Gritzali M., Stafford D.W.;
RT "Nucleotide sequence and deduced primary structure of cellobiohydrolase II
RT from Trichoderma reesei.";
RL Biotechnology (N.Y.) 5:274-278(1987).
RN [3]
RP PROTEIN SEQUENCE OF 25-44, PYROGLUTAMATE FORMATION AT GLN-25, FUNCTION,
RP CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 26921 / CBS 392.92 / QM9414;
RX DOI=10.1016/0014-5793(80)81006-4;
RA Faegerstam L.G., Pettersson L.G.;
RT "The 1,4-beta-glucan cellobiohydrolases of Trichoderma reesei QM 9414.";
RL FEBS Lett. 119:97-100(1980).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 107-471, AND MUTAGENESIS OF
RP ASP-199 AND ASP-245.
RX PubMed=2377893; DOI=10.1126/science.2377893;
RA Rouvinen J., Bergfors T., Teeri T.T., Knowles J.K.C., Jones T.A.;
RT "Three-dimensional structure of cellobiohydrolase II from Trichoderma
RT reesei.";
RL Science 249:380-386(1990).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 107-471, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT THR-111; THR-121; SER-130; SER-133; SER-134; SER-139;
RP THR-146; ASN-313 AND ASN-334.
RX PubMed=8875646; DOI=10.1093/protein/9.8.691;
RA Koivula A., Reinikainen T., Ruohonen L., Valkeajaervi A., Claeyssens M.,
RA Teleman O., Kleywegt G.J., Szardenings M., Rouvinen J., Jones T.A.,
RA Teeri T.T.;
RT "The active site of Trichoderma reesei cellobiohydrolase II: the role of
RT tyrosine 169.";
RL Protein Eng. 9:691-699(1996).
RN [6] {ECO:0007744|PDB:1HGW, ECO:0007744|PDB:1HGY}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 107-471, ACTIVE SITE,
RP GLYCOSYLATION AT THR-111; THR-121; SER-130; SER-133; SER-134; SER-139;
RP THR-146; ASN-313 AND ASN-334, DISULFIDE BONDS, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=12188666; DOI=10.1021/ja012659q;
RA Koivula A., Ruohonen L., Wohlfahrt G., Reinikainen T., Teeri T.T.,
RA Piens K., Claeyssens M., Weber M., Vasella A., Becker D., Sinnott M.L.,
RA Zou J.Y., Kleywegt G.J., Szardenings M., Stahlberg J., Jones T.A.;
RT "The active site of cellobiohydrolase Cel6A from Trichoderma reesei: the
RT roles of aspartic acids D221 and D175.";
RL J. Am. Chem. Soc. 124:10015-10024(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 (Ref.3). The degradation of cellulose involves an interplay
CC between different cellulolytic enzymes. Hydrolysis starts with
CC endoglucanases (EGs), which cut internal beta-1,4-glucosidic bonds in
CC cellulose to reduce the polymerization degree of the substrate and
CC create new chain ends for exocellobiohydrolases (CBHs). The CBHs
CC release the disaccharide cellobiose from the non-reducing end of the
CC cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the
CC cellobiose and other short cello-oligosaccharides into glucose units
CC (Probable). {ECO:0000269|Ref.3, ECO:0000305}.
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:0000269|Ref.3};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 uM for cellotriose {ECO:0000269|PubMed:12188666};
CC KM=2.6 uM for cellotetraose {ECO:0000269|PubMed:12188666};
CC KM=1.3 uM for cellopentaose {ECO:0000269|PubMed:12188666};
CC KM=14 uM for cellohexaose {ECO:0000269|PubMed:12188666};
CC Note=kcat is 0.06 sec(-1) with cellotriose as substrate, 4.1 sec(-1)
CC with cellotetraose as substrate, 1.1 sec(-1) with cellopentaose as
CC substrate and 14 sec(-1) with cellopentaose as substrate.
CC {ECO:0000269|PubMed:12188666};
CC pH dependence:
CC Optimum pH is 4-6. {ECO:0000269|PubMed:12188666};
CC -!- INTERACTION:
CC P07987; P07987: cbh2; NbExp=2; IntAct=EBI-8155616, EBI-8155616;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.3}.
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. {ECO:0000305}.
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:0000250|UniProtKB:A0A024SH76}.
CC -!- MISCELLANEOUS: T.reesei produces two different exocellobiohydrolases.
CC They are unique in that they can hydrolyze crystalline cellulose in the
CC absence of endoglucanases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B) family.
CC {ECO:0000305}.
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DR EMBL; M16190; AAA34210.1; -; Genomic_DNA.
DR EMBL; M55080; AAA72922.1; -; Genomic_DNA.
DR PIR; A26160; A26160.
DR PDB; 1CB2; X-ray; 2.00 A; A/B=107-471.
DR PDB; 1HGW; X-ray; 2.10 A; A/B=107-471.
DR PDB; 1HGY; X-ray; 2.20 A; A/B=107-471.
DR PDB; 1QJW; X-ray; 1.90 A; A/B=107-471.
DR PDB; 1QK0; X-ray; 2.10 A; A/B=109-471.
DR PDB; 1QK2; X-ray; 2.00 A; A/B=109-471.
DR PDB; 3CBH; X-ray; 2.00 A; A=107-471.
DR PDB; 4AU0; X-ray; 1.70 A; A/B=109-471.
DR PDB; 4AX6; X-ray; 2.30 A; A/B=109-471.
DR PDB; 4AX7; X-ray; 1.70 A; A/B/C/D=109-471.
DR PDB; 4I5R; X-ray; 1.50 A; A=158-331, A=425-471.
DR PDB; 4I5U; X-ray; 1.22 A; A=158-331, A=425-471.
DR PDBsum; 1CB2; -.
DR PDBsum; 1HGW; -.
DR PDBsum; 1HGY; -.
DR PDBsum; 1QJW; -.
DR PDBsum; 1QK0; -.
DR PDBsum; 1QK2; -.
DR PDBsum; 3CBH; -.
DR PDBsum; 4AU0; -.
DR PDBsum; 4AX6; -.
DR PDBsum; 4AX7; -.
DR PDBsum; 4I5R; -.
DR PDBsum; 4I5U; -.
DR AlphaFoldDB; P07987; -.
DR SMR; P07987; -.
DR MINT; P07987; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH6; Glycoside Hydrolase Family 6.
DR CLAE; CBH6B_TRIRE; -.
DR iPTMnet; P07987; -.
DR VEuPathDB; FungiDB:TrQ_010160; -.
DR OMA; NTPQAYW; -.
DR BRENDA; 3.2.1.176; 6451.
DR BRENDA; 3.2.1.91; 6451.
DR EvolutionaryTrace; P07987; -.
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:0042802; F:identical protein binding; IPI:IntAct.
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 3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Pyrrolidone carboxylic acid;
KW Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT PROPEP 19..24
FT /evidence="ECO:0000269|Ref.3"
FT /id="PRO_0000441277"
FT CHAIN 25..471
FT /note="Exoglucanase 2"
FT /id="PRO_0000007911"
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:0000305"
FT REGION 107..471
FT /note="Catalytic"
FT /evidence="ECO:0000305|PubMed:2377893"
FT ACT_SITE 245
FT /note="Proton donor"
FT /evidence="ECO:0000269|PubMed:12188666"
FT SITE 38
FT /note="Not glycosylated"
FT /evidence="ECO:0000250|UniProtKB:A0A024SH76"
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:0000269|PubMed:2377893"
FT MOD_RES 25
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|Ref.2"
FT CARBOHYD 111
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:12188666,
FT ECO:0000269|PubMed:8875646"
FT CARBOHYD 121
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:12188666,
FT ECO:0000269|PubMed:8875646"
FT CARBOHYD 130
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:12188666,
FT ECO:0000269|PubMed:8875646"
FT CARBOHYD 133
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:12188666,
FT ECO:0000269|PubMed:8875646"
FT CARBOHYD 134
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:12188666,
FT ECO:0000269|PubMed:8875646"
FT CARBOHYD 139
FT /note="O-linked (Man...) serine"
FT /evidence="ECO:0000269|PubMed:12188666,
FT ECO:0000269|PubMed:8875646"
FT CARBOHYD 146
FT /note="O-linked (Man...) threonine"
FT /evidence="ECO:0000269|PubMed:12188666,
FT ECO:0000269|PubMed:8875646"
FT CARBOHYD 313
FT /note="N-linked (GlcNAc) asparagine"
FT /evidence="ECO:0000269|PubMed:12188666,
FT ECO:0000269|PubMed:8875646"
FT CARBOHYD 334
FT /note="N-linked (GlcNAc...) (high mannose) asparagine"
FT /evidence="ECO:0000269|PubMed:12188666,
FT ECO:0000269|PubMed:8875646"
FT DISULFID 200..259
FT /evidence="ECO:0000269|PubMed:12188666,
FT ECO:0000269|PubMed:8875646"
FT DISULFID 392..439
FT /evidence="ECO:0000269|PubMed:12188666,
FT ECO:0000269|PubMed:8875646"
FT MUTAGEN 199
FT /note="D->A: 20% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:2377893"
FT MUTAGEN 245
FT /note="D->A: No measurable activity."
FT /evidence="ECO:0000269|PubMed:2377893"
FT CONFLICT 359
FT /note="P -> R (in Ref. 2; AAA72922)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="P -> A (in Ref. 2; AAA72922)"
FT /evidence="ECO:0000305"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:4AU0"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:1QJW"
FT HELIX 126..135
FT /evidence="ECO:0007829|PDB:4AU0"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:4AU0"
FT HELIX 142..151
FT /evidence="ECO:0007829|PDB:4AU0"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:4I5R"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:4I5U"
FT HELIX 166..181
FT /evidence="ECO:0007829|PDB:4I5U"
FT STRAND 186..192
FT /evidence="ECO:0007829|PDB:4I5U"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1CB2"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:4I5U"
FT HELIX 215..232
FT /evidence="ECO:0007829|PDB:4I5U"
FT TURN 233..235
FT /evidence="ECO:0007829|PDB:4I5U"
FT STRAND 238..242
FT /evidence="ECO:0007829|PDB:4I5U"
FT STRAND 244..246
FT /evidence="ECO:0007829|PDB:1QJW"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:4I5U"
FT HELIX 257..276
FT /evidence="ECO:0007829|PDB:4I5U"
FT STRAND 282..287
FT /evidence="ECO:0007829|PDB:4I5U"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:4I5U"
FT HELIX 297..313
FT /evidence="ECO:0007829|PDB:4I5U"
FT STRAND 320..326
FT /evidence="ECO:0007829|PDB:4I5U"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:4AU0"
FT HELIX 350..363
FT /evidence="ECO:0007829|PDB:4AU0"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:4AU0"
FT STRAND 379..382
FT /evidence="ECO:0007829|PDB:4AU0"
FT STRAND 392..396
FT /evidence="ECO:0007829|PDB:4AU0"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:1QK2"
FT STRAND 410..416
FT /evidence="ECO:0007829|PDB:4AU0"
FT STRAND 432..434
FT /evidence="ECO:0007829|PDB:1HGY"
FT HELIX 437..440
FT /evidence="ECO:0007829|PDB:4I5U"
FT HELIX 456..464
FT /evidence="ECO:0007829|PDB:4I5U"
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
