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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 – 14311 Publication
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-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Add
BLAST
Chaini18 – 513496Exoglucanase 1PRO_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...)Sequence Analysis
Disulfide bondi67 ↔ 88
Disulfide bondi78 ↔ 84
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi155 ↔ 414
Disulfide bondi189 ↔ 227
Disulfide bondi193 ↔ 226
Disulfide bondi247 ↔ 273
Disulfide bondi255 ↔ 260
Disulfide bondi278 ↔ 348
Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi401 – 4011N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi485 ↔ 502
Disulfide bondi496 ↔ 512

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Structurei

Secondary structure

1
513
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi30 – 367Combined sources
Beta strandi42 – 5110Combined sources
Helixi53 – 553Combined sources
Beta strandi58 – 603Combined sources
Beta strandi66 – 694Combined sources
Turni75 – 773Combined sources
Helixi81 – 877Combined sources
Beta strandi88 – 903Combined sources
Helixi95 – 995Combined sources
Beta strandi101 – 1044Combined sources
Beta strandi107 – 12115Combined sources
Beta strandi123 – 1308Combined sources
Beta strandi136 – 1383Combined sources
Beta strandi142 – 1498Combined sources
Beta strandi157 – 1648Combined sources
Turni168 – 1747Combined sources
Helixi182 – 1843Combined sources
Beta strandi198 – 2003Combined sources
Beta strandi222 – 2265Combined sources
Beta strandi229 – 2357Combined sources
Beta strandi240 – 2456Combined sources
Beta strandi247 – 2493Combined sources
Beta strandi253 – 2564Combined sources
Helixi257 – 2604Combined sources
Turni262 – 2643Combined sources
Beta strandi265 – 2673Combined sources
Beta strandi268 – 2736Combined sources
Turni282 – 2865Combined sources
Beta strandi290 – 2945Combined sources
Beta strandi297 – 3004Combined sources
Beta strandi305 – 3117Combined sources
Beta strandi317 – 3237Combined sources
Beta strandi326 – 3294Combined sources
Beta strandi333 – 3353Combined sources
Beta strandi338 – 3436Combined sources
Helixi345 – 35511Combined sources
Helixi359 – 3624Combined sources
Helixi365 – 37410Combined sources
Beta strandi375 – 38511Combined sources
Turni387 – 3915Combined sources
Helixi392 – 3954Combined sources
Beta strandi396 – 3994Combined sources
Beta strandi412 – 4143Combined sources
Helixi421 – 4277Combined sources
Beta strandi432 – 44211Combined sources
Turni479 – 4824Combined sources
Beta strandi483 – 4897Combined sources
Beta strandi498 – 5003Combined sources
Beta strandi502 – 5065Combined sources
Beta strandi509 – 5124Combined sources

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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62694.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini477 – 51337CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 453436CatalyticAdd
BLAST
Regioni454 – 47724LinkerAdd
BLAST

Sequence similaritiesi

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG85664.

Family and domain databases

Gene3Di2.70.100.10. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR013320. ConA-like_dom.
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

« Hide

        10         20         30         40         50
MYRKLAVISA FLATARAQSA CTLQSETHPP LTWQKCSSGG TCTQQTGSVV
60 70 80 90 100
IDANWRWTHA TNSSTNCYDG NTWSSTLCPD NETCAKNCCL DGAAYASTYG
110 120 130 140 150
VTTSGNSLSI GFVTQSAQKN VGARLYLMAS DTTYQEFTLL GNEFSFDVDV
160 170 180 190 200
SQLPCGLNGA LYFVSMDADG GVSKYPTNTA GAKYGTGYCD SQCPRDLKFI
210 220 230 240 250
NGQANVEGWE PSSNNANTGI GGHGSCCSEM DIWEANSISE ALTPHPCTTV
260 270 280 290 300
GQEICEGDGC GGTYSDNRYG GTCDPDGCDW NPYRLGNTSF YGPGSSFTLD
310 320 330 340 350
TTKKLTVVTQ FETSGAINRY YVQNGVTFQQ PNAELGSYSG NELNDDYCTA
360 370 380 390 400
EEAEFGGSSF SDKGGLTQFK KATSGGMVLV MSLWDDYYAN MLWLDSTYPT
410 420 430 440 450
NETSSTPGAV RGSCSTSSGV PAQVESQSPN AKVTFSNIKF GPIGSTGNPS
460 470 480 490 500
GGNPPGGNRG TTTTRRPATT TGSSPGPTQS HYGQCGGIGY SGPTVCASGT
510
TCQVLNPYYS QCL
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.
IPR013320. ConA-like_dom.
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: October 29, 2014
This is version 70 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