GUX1_TRIHA
ID GUX1_TRIHA Reviewed; 505 AA.
AC Q9P8P3;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Exoglucanase 1;
DE EC=3.2.1.91;
DE AltName: Full=1,4-beta-cellobiohydrolase;
DE AltName: Full=Cellobiohydrolase 7A;
DE Short=Cel7A;
DE AltName: Full=Exocellobiohydrolase I;
DE Short=CBHI;
DE AltName: Full=Exoglucanase I;
DE Flags: Precursor;
GN Name=cbh1;
OS Trichoderma harzianum (Hypocrea lixii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=5544;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FP 108;
RA Guilfoile P.G., Burns R., Gu Z.-Y., Amundson M., Chang F.-H.;
RT "Cloning and sequencing of a cellobiohydrolase gene from Trichoderma
RT harzianum FP 108.";
RL J. Minn. Acad. Sci. 64:18-22(1999).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=IOC 3844;
RX PubMed=21876370; DOI=10.4014/jmb.1010.10037;
RA Colussi F., Serpa V., Delabona P.D.S., Manzine L.R., Voltatodio M.L.,
RA Alves R., Mello B.L., Pereira N. Jr., Farinas C.S., Golubev A.M.,
RA Santos M.A., Polikarpov I.;
RT "Purification, and biochemical and biophysical characterization of
RT cellobiohydrolase I from Trichoderma harzianum IOC 3844.";
RL J. Microbiol. Biotechnol. 21:808-817(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) OF 19-443, FUNCTION, CATALYTIC
RP ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION AT ASN-126 AND
RP ASN-397, PYROGLUTAMATE FORMATION AT GLN-18, AND DISULFIDE BONDS.
RC STRAIN=IOC 3844;
RX PubMed=23114223; DOI=10.1111/febs.12049;
RA Textor L.C., Colussi F., Silveira R.L., Serpa V., de Mello B.L.,
RA Muniz J.R., Squina F.M., Pereira N. Jr., Skaf M.S., Polikarpov I.;
RT "Joint X-ray crystallographic and molecular dynamics study of
RT cellobiohydrolase I from Trichoderma harzianum: deciphering the structural
RT features of cellobiohydrolase catalytic activity.";
RL FEBS J. 280:56-69(2013).
CC -!- FUNCTION: Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of
CC 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide
CC cellobiose (PubMed:21876370). The degradation of cellulose involves an
CC interplay between different cellulolytic enzymes. Hydrolysis starts
CC with endoglucanases (EGs), which cut internal beta-1,4-glucosidic bonds
CC in 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|PubMed:21876370, 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|PubMed:21876370,
CC ECO:0000269|PubMed:23114223};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.4 mM for p-nitrophenyl-D-cellobioside
CC {ECO:0000269|PubMed:23114223};
CC KM=3.7 mM for 2-chloro-4-nitrophenyl-beta-lactoside
CC {ECO:0000269|PubMed:23114223};
CC Vmax=0.016 mmol/min/mg enzyme for p-nitrophenyl-D-cellobioside
CC {ECO:0000269|PubMed:23114223};
CC Vmax=0.031 mmol/min/mg enzyme for 2-chloro-4-nitrophenyl-beta-
CC lactoside {ECO:0000269|PubMed:23114223};
CC Note=kcat is 23.2 min(-1) with p-nitrophenyl-D-cellobioside as
CC substrate and 44.6 min(-1) with 2-chloro-4-nitrophenyl-beta-lactoside
CC as substrate. {ECO:0000269|PubMed:23114223};
CC pH dependence:
CC Optimum pH is 5.0. {ECO:0000269|PubMed:21876370};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:21876370};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21876370}.
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:P62694}.
CC -!- PTM: O-glycosylated. O-glycosylation of the cellulase linker provides
CC protection from proteolysis. Linker glycans also contribute to binding
CC affinity of cellobiohydrolases to cellulose.
CC {ECO:0000250|UniProtKB:P62694}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC {ECO:0000305}.
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DR EMBL; AF223252; AAF36391.1; -; Genomic_DNA.
DR PDB; 2Y9N; X-ray; 2.89 A; A=19-449.
DR PDB; 2YOK; X-ray; 1.67 A; A=19-443.
DR PDBsum; 2Y9N; -.
DR PDBsum; 2YOK; -.
DR AlphaFoldDB; Q9P8P3; -.
DR SMR; Q9P8P3; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH7; Glycoside Hydrolase Family 7.
DR iPTMnet; Q9P8P3; -.
DR BRENDA; 3.2.1.176; 6445.
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 CDD; cd07999; GH7_CBH_EG; 1.
DR Gene3D; 2.70.100.10; -; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001722; Glyco_hydro_7.
DR InterPro; IPR037019; Glyco_hydro_7_sf.
DR PANTHER; PTHR33753; PTHR33753; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF00840; Glyco_hydro_7; 1.
DR PRINTS; PR00734; GLHYDRLASE7.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cellulose degradation;
KW Disulfide bond; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Pyrrolidone carboxylic acid; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..505
FT /note="Exoglucanase 1"
FT /id="PRO_0000007925"
FT DOMAIN 469..505
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 18..449
FT /note="Catalytic"
FT /evidence="ECO:0000305|PubMed:21876370"
FT REGION 399..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..468
FT /note="Linker"
FT /evidence="ECO:0000305"
FT ACT_SITE 225
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:23114223"
FT ACT_SITE 230
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:23114223"
FT MOD_RES 18
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:23114223"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23114223"
FT CARBOHYD 283
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23114223"
FT CARBOHYD 397
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:23114223"
FT DISULFID 21..88
FT /evidence="ECO:0000269|PubMed:23114223"
FT DISULFID 36..41
FT /evidence="ECO:0000269|PubMed:23114223"
FT DISULFID 66..87
FT /evidence="ECO:0000269|PubMed:23114223"
FT DISULFID 77..83
FT /evidence="ECO:0000269|PubMed:23114223"
FT DISULFID 151..410
FT /evidence="ECO:0000269|PubMed:23114223"
FT DISULFID 185..223
FT /evidence="ECO:0000269|PubMed:23114223"
FT DISULFID 189..222
FT /evidence="ECO:0000269|PubMed:23114223"
FT DISULFID 243..269
FT /evidence="ECO:0000269|PubMed:23114223"
FT DISULFID 251..256
FT /evidence="ECO:0000269|PubMed:23114223"
FT DISULFID 274..344
FT /evidence="ECO:0000269|PubMed:23114223"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 40..50
FT /evidence="ECO:0007829|PDB:2YOK"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2YOK"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:2YOK"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2YOK"
FT HELIX 94..98
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 106..113
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:2YOK"
FT TURN 164..170
FT /evidence="ECO:0007829|PDB:2YOK"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 218..222
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 225..231
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 243..247
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:2YOK"
FT HELIX 253..256
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 258..262
FT /evidence="ECO:0007829|PDB:2Y9N"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:2YOK"
FT TURN 278..282
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 301..307
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 313..319
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 322..325
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 334..340
FT /evidence="ECO:0007829|PDB:2YOK"
FT HELIX 341..351
FT /evidence="ECO:0007829|PDB:2YOK"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:2YOK"
FT HELIX 361..370
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 373..380
FT /evidence="ECO:0007829|PDB:2YOK"
FT TURN 383..387
FT /evidence="ECO:0007829|PDB:2YOK"
FT HELIX 388..391
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 408..410
FT /evidence="ECO:0007829|PDB:2Y9N"
FT TURN 412..415
FT /evidence="ECO:0007829|PDB:2Y9N"
FT HELIX 417..423
FT /evidence="ECO:0007829|PDB:2YOK"
FT STRAND 428..438
FT /evidence="ECO:0007829|PDB:2YOK"
SQ SEQUENCE 505 AA; 53216 MW; 52930722F97D7BF0 CRC64;
MYRKLAVISA FLAAARAQQV CTQQAETHPP LTWQKCTASG CTPQQGSVVL DANWRWTHDT
KSTTNCYDGN TWSSTLCPDD ATCAKNCCLD GANYSGTYGV TTSGDALTLQ FVTASNVGSR
LYLMANDSTY QEFTLSGNEF SFDVDVSQLP CGLNGALYFV SMDADGGQSK YPGNAAGAKY
GTGYCDSQCP RDLKFINGQA NVEGWEPSSN NANTGVGGHG SCCSEMDIWE ANSISEALTP
HPCETVGQTM CSGDSCGGTY SNDRYGGTCD PDGCDWNPYR LGNTSFYGPG SSFALDTTKK
LTVVTQFATD GSISRYYVQN GVKFQQPNAQ VGSYSGNTIN TDYCAAEQTA FGGTSFTDKG
GLAQINKAFQ GGMVLVMSLW DDYAVNMLWL DSTYPTNATA STPGAKRGSC STSSGVPAQV
EAQSPNSKVI YSNIRFGPIG STGGNTGSNP PGTSTTRAPP SSTGSSPTAT QTHYGQCGGT
GWTGPTRCAS GYTCQVLNPF YSQCL
