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 27-MAR-2024, entry version 170. 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}. 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; 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 GlyCosmos; P07987; 9 sites, No reported glycans. DR iPTMnet; P07987; -. DR VEuPathDB; FungiDB:TrQ_010160; -. DR OMA; EVHTLAM; -. 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, 4-beta cellobiohydrolase; 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; -; 1. DR PANTHER; PTHR34876:SF4; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE C-RELATED; 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; SSF57180; Cellulose-binding domain; 1. DR SUPFAM; SSF51989; Glycosyl hydrolases family 6, cellulases; 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 //