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P62694

- GUX1_HYPJE

UniProt

P62694 - GUX1_HYPJE

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Protein
Exoglucanase 1
Gene
cbh1
Organism
Hypocrea jecorina (Trichoderma reesei)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.

Catalytic activityi

Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei143 – 1431 Inferred
Active sitei229 – 2291Nucleophile1 Publication
Active sitei234 – 2341Proton donor1 Publication

GO - Molecular functioni

  1. cellulose 1,4-beta-cellobiosidase activity Source: UniProtKB-EC
  2. cellulose binding Source: InterPro

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16499.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPiCBH7A_TRIRE.

Names & Taxonomyi

Protein namesi
Recommended name:
Exoglucanase 1 (EC:3.2.1.91)
Alternative name(s):
1,4-beta-cellobiohydrolase
Exocellobiohydrolase I
Short name:
CBHI
Exoglucanase I
Gene namesi
Name:cbh1
OrganismiHypocrea jecorina (Trichoderma reesei)
Taxonomic identifieri51453 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717
Add
BLAST
Chaini18 – 513496Exoglucanase 1
PRO_0000007927Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181Pyrrolidone carboxylic acid
Disulfide bondi21 ↔ 89
Disulfide bondi36 ↔ 42
Glycosylationi62 – 621N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi67 ↔ 88
Disulfide bondi78 ↔ 84
Glycosylationi81 – 811N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi155 ↔ 414
Disulfide bondi189 ↔ 227
Disulfide bondi193 ↔ 226
Disulfide bondi247 ↔ 273
Disulfide bondi255 ↔ 260
Disulfide bondi278 ↔ 348
Glycosylationi287 – 2871N-linked (GlcNAc...) Reviewed prediction
Glycosylationi401 – 4011N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi485 ↔ 502
Disulfide bondi496 ↔ 512

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 367
Beta strandi42 – 5110
Helixi53 – 553
Beta strandi58 – 603
Beta strandi66 – 694
Turni75 – 773
Helixi81 – 877
Beta strandi88 – 903
Helixi95 – 995
Beta strandi101 – 1044
Beta strandi107 – 12115
Beta strandi123 – 1308
Beta strandi136 – 1383
Beta strandi142 – 1498
Beta strandi157 – 1648
Turni168 – 1747
Helixi182 – 1843
Beta strandi198 – 2003
Beta strandi222 – 2265
Beta strandi229 – 2357
Beta strandi240 – 2456
Beta strandi247 – 2493
Beta strandi253 – 2564
Helixi257 – 2604
Turni262 – 2643
Beta strandi265 – 2673
Beta strandi268 – 2736
Turni282 – 2865
Beta strandi290 – 2945
Beta strandi297 – 3004
Beta strandi305 – 3117
Beta strandi317 – 3237
Beta strandi326 – 3294
Beta strandi333 – 3353
Beta strandi338 – 3436
Helixi345 – 35511
Helixi359 – 3624
Helixi365 – 37410
Beta strandi375 – 38511
Turni387 – 3915
Helixi392 – 3954
Beta strandi396 – 3994
Beta strandi412 – 4143
Helixi421 – 4277
Beta strandi432 – 44211
Turni479 – 4824
Beta strandi483 – 4897
Beta strandi498 – 5003
Beta strandi502 – 5065
Beta strandi509 – 5124

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1AZ6NMR-A478-513[»]
1AZHNMR-A478-513[»]
1AZJNMR-A478-513[»]
1AZKNMR-A478-513[»]
1CBHNMR-A478-513[»]
1CELX-ray1.80A/B19-451[»]
1DY4X-ray1.90A19-451[»]
1EGNX-ray1.60A18-451[»]
1Q2BX-ray1.60A18-451[»]
1Q2EX-ray1.75A/B19-451[»]
2CBHNMR-A478-513[»]
2CELX-ray2.00A/B19-451[»]
2V3IX-ray1.05A19-451[»]
2V3RX-ray1.60A19-451[»]
3CELX-ray2.00A19-451[»]
4C4CX-ray1.45A19-451[»]
4C4DX-ray1.32A19-451[»]
4CELX-ray2.20A/B19-451[»]
5CELX-ray1.90A19-451[»]
6CELX-ray1.70A19-451[»]
7CELX-ray1.90A19-451[»]
8CELmodel-A18-451[»]
ProteinModelPortaliP62694.
SMRiP62694. Positions 18-451, 478-513.

Miscellaneous databases

EvolutionaryTraceiP62694.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini477 – 51337CBM1
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 453436Catalytic
Add
BLAST
Regioni454 – 47724Linker
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG85664.

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR008985. ConA-like_lec_gl_sf.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSiPR00734. GLHYDRLASE7.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P62694-1 [UniParc]FASTAAdd to Basket

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MYRKLAVISA FLATARAQSA CTLQSETHPP LTWQKCSSGG TCTQQTGSVV    50
IDANWRWTHA TNSSTNCYDG NTWSSTLCPD NETCAKNCCL DGAAYASTYG 100
VTTSGNSLSI GFVTQSAQKN VGARLYLMAS DTTYQEFTLL GNEFSFDVDV 150
SQLPCGLNGA LYFVSMDADG GVSKYPTNTA GAKYGTGYCD SQCPRDLKFI 200
NGQANVEGWE PSSNNANTGI GGHGSCCSEM DIWEANSISE ALTPHPCTTV 250
GQEICEGDGC GGTYSDNRYG GTCDPDGCDW NPYRLGNTSF YGPGSSFTLD 300
TTKKLTVVTQ FETSGAINRY YVQNGVTFQQ PNAELGSYSG NELNDDYCTA 350
EEAEFGGSSF SDKGGLTQFK KATSGGMVLV MSLWDDYYAN MLWLDSTYPT 400
NETSSTPGAV RGSCSTSSGV PAQVESQSPN AKVTFSNIKF GPIGSTGNPS 450
GGNPPGGNRG TTTTRRPATT TGSSPGPTQS HYGQCGGIGY SGPTVCASGT 500
TCQVLNPYYS QCL 513
Length:513
Mass (Da):54,073
Last modified:July 21, 1986 - v1
Checksum:i9F5C0A8A854F2C12
GO

Sequence databases

PIRiA00902. EUTQI.

Cross-referencesi

Sequence databases

PIRi A00902. EUTQI.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1AZ6 NMR - A 478-513 [» ]
1AZH NMR - A 478-513 [» ]
1AZJ NMR - A 478-513 [» ]
1AZK NMR - A 478-513 [» ]
1CBH NMR - A 478-513 [» ]
1CEL X-ray 1.80 A/B 19-451 [» ]
1DY4 X-ray 1.90 A 19-451 [» ]
1EGN X-ray 1.60 A 18-451 [» ]
1Q2B X-ray 1.60 A 18-451 [» ]
1Q2E X-ray 1.75 A/B 19-451 [» ]
2CBH NMR - A 478-513 [» ]
2CEL X-ray 2.00 A/B 19-451 [» ]
2V3I X-ray 1.05 A 19-451 [» ]
2V3R X-ray 1.60 A 19-451 [» ]
3CEL X-ray 2.00 A 19-451 [» ]
4C4C X-ray 1.45 A 19-451 [» ]
4C4D X-ray 1.32 A 19-451 [» ]
4CEL X-ray 2.20 A/B 19-451 [» ]
5CEL X-ray 1.90 A 19-451 [» ]
6CEL X-ray 1.70 A 19-451 [» ]
7CEL X-ray 1.90 A 19-451 [» ]
8CEL model - A 18-451 [» ]
ProteinModelPortali P62694.
SMRi P62694. Positions 18-451, 478-513.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM1. Carbohydrate-Binding Module Family 1.
GH7. Glycoside Hydrolase Family 7.
mycoCLAPi CBH7A_TRIRE.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi NOG85664.

Enzyme and pathway databases

BioCyci MetaCyc:MONOMER-16499.

Miscellaneous databases

EvolutionaryTracei P62694.

Family and domain databases

Gene3Di 2.70.100.10. 1 hit.
InterProi IPR000254. Cellulose-bd_dom_fun.
IPR008985. ConA-like_lec_gl_sf.
IPR001722. Glyco_hydro_7.
[Graphical view ]
Pfami PF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view ]
PRINTSi PR00734. GLHYDRLASE7.
ProDomi PD001821. CBD_fun. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00236. fCBD. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEi PS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning of exo-cellobiohydrolase I derived from Trichoderma reesei strain L27."
    Shoemaker S., Schweickart V., Ladner M., Gelfand D., Kwok S., Myambo K., Innis M.
    Biotechnology (N.Y.) 1:691-696(1983)
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: L27.
  2. "Identification of a functionally important carboxyl group in cellobiohydrolase I from Trichoderma reesei."
    Tomme P., Clayssens M.
    FEBS Lett. 243:239-243(1989)
    Cited for: ACTIVE SITE.
    Strain: ATCC 26921 / CBS 392.92 / QM9414.
  3. "The three-dimensional crystal structure of the catalytic core of cellobiohydrolase I from Trichoderma reesei."
    Divne C., Staahlberg J., Reinikainen T., Ruohonen L., Pettersson G., Knowles J.K.C., Teeri T.T., Jones T.A.
    Science 265:524-528(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 18-452.
  4. "High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei."
    Divne C., Staahlberg J., Teeri T.T., Jones T.A.
    J. Mol. Biol. 275:309-325(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 18-452.
    Strain: ATCC 26921 / CBS 392.92 / QM9414.
  5. "Determination of the three-dimensional solution structure of the C-terminal domain of cellobiohydrolase I from Trichoderma reesei. A study using nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing."
    Kraulis P.J., Clore G.M., Nilges M., Jones T.A., Pettersson G., Knowles J., Gronenborn A.M.
    Biochemistry 28:7241-7257(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 478-513.
  6. "Three-dimensional structures of three engineered cellulose-binding domains of cellobiohydrolase I from Trichoderma reesei."
    Mattinen M.L., Kontteli M., Kerovuo J., Linder M., Annila A., Lindeberg G., Reinikainen T., Drakenberg T.
    Protein Sci. 6:294-303(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 478-513.

Entry informationi

Entry nameiGUX1_HYPJE
AccessioniPrimary (citable) accession number: P62694
Secondary accession number(s): P00725
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

T.reesei produces two different exocellobiohydrolases. They are unique in that they can hydrolyze crystalline cellulose in the absence of endoglucanases.

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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