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Protein

Exoglucanase 1

Gene

cbh1

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

Functioni

Exocellobiohydrolases (CBH) that catalyzes the hydrolysis of 1,4-beta-D-glucosidic bonds in cellulose to release the disaccharide cellobiose (Ref. 4). The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydolysis starts with endoglucanases (EGs), which cut internal beta-1,4-glucosidic bonds in cellulose to reduce the polymerization degree of the substrate and create new chain ends for exocellobiohydrolases (CBHs). The CBHs release the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short cello-oligosaccharides into glucose units (Probable).Curated1 Publication

Miscellaneous

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

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei229Nucleophile1 Publication1 Publication1
Active sitei234Proton donor/acceptor1 Publication1 Publication1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Cellulose degradation, Polysaccharide degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16499.
BRENDAi3.2.1.176. 6451.
3.2.1.91. 6451.

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:3.2.1.911 Publication)
Alternative name(s):
1,4-beta-cellobiohydrolase
Cellobiohydrolase 7A
Short name:
Cel7A
Exocellobiohydrolase I
Short name:
CBHI
Exoglucanase I
Gene namesi
Name:cbh1
OrganismiHypocrea jecorina (Trichoderma reesei)
Taxonomic identifieri51453 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 172 PublicationsAdd BLAST17
ChainiPRO_000000792718 – 513Exoglucanase 1Add BLAST496

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei18Pyrrolidone carboxylic acidCombined sources2 Publications1
Disulfide bondi21 ↔ 893 Publications
Disulfide bondi36 ↔ 423 Publications
Glycosylationi62N-linked (GlcNAc) asparagine1 Publication1
Disulfide bondi67 ↔ 883 Publications
Disulfide bondi78 ↔ 843 Publications
Disulfide bondi155 ↔ 4143 Publications
Disulfide bondi189 ↔ 2273 Publications
Disulfide bondi193 ↔ 2263 Publications
Disulfide bondi247 ↔ 2733 Publications
Disulfide bondi255 ↔ 2603 Publications
Disulfide bondi278 ↔ 3483 Publications
Glycosylationi287N-linked (GlcNAc) asparagine4 Publications1
Glycosylationi401N-linked (GlcNAc) asparagine3 Publications1
Glycosylationi461O-linked (Man) threonine1 Publication1
Glycosylationi462O-linked (Man...) threonine1 Publication1
Glycosylationi463O-linked (Man...) threonine1 Publication1
Glycosylationi464O-linked (Man...) threonine1 Publication1
Glycosylationi469O-linked (Man) threonine1 Publication1
Glycosylationi470O-linked (Man...) threonine1 Publication1
Glycosylationi471O-linked (Man...) threonine1 Publication1
Glycosylationi473O-linked (Man) serine1 Publication1
Glycosylationi474O-linked (Man) serine1 Publication1
Glycosylationi478O-linked (Man) threonine2 Publications1
Glycosylationi480O-linked (Man) serine2 Publications1
Disulfide bondi485 ↔ 5023 Publications
Glycosylationi491O-linked (Man) serine1 Publication1
Disulfide bondi496 ↔ 5123 Publications

Post-translational modificationi

N-glycosylated. The catalytic core domain comprises three N-linked glycans which each consist of a single N-acetylglucosamine residue.1 Publication
O-glycosylated. Within the linker domain, all 8 threonines are variably glycosylated with between at least one, and up to three, mannose residues per site. All serines in this domain are at least partially glycosylated with a single mannose residue (PubMed:9746354). O-glycosylation of the cellulase linker provides protection from proteolysis. Linker glycans also contribute to binding affinity of cellobiohydrolases to cellulose (Probable).1 Publication1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei81Not glycosylated1 Publication1

Keywords - PTMi

Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Structurei

Secondary structure

1513
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi19 – 21Combined sources3
Beta strandi30 – 36Combined sources7
Beta strandi42 – 51Combined sources10
Helixi53 – 55Combined sources3
Beta strandi58 – 60Combined sources3
Beta strandi66 – 69Combined sources4
Turni75 – 77Combined sources3
Helixi81 – 87Combined sources7
Beta strandi88 – 90Combined sources3
Helixi95 – 99Combined sources5
Beta strandi101 – 104Combined sources4
Beta strandi107 – 121Combined sources15
Beta strandi123 – 130Combined sources8
Beta strandi136 – 138Combined sources3
Beta strandi142 – 149Combined sources8
Beta strandi157 – 164Combined sources8
Turni168 – 174Combined sources7
Helixi182 – 184Combined sources3
Beta strandi198 – 200Combined sources3
Beta strandi203 – 205Combined sources3
Beta strandi222 – 226Combined sources5
Beta strandi229 – 235Combined sources7
Beta strandi240 – 245Combined sources6
Beta strandi247 – 249Combined sources3
Beta strandi253 – 256Combined sources4
Helixi257 – 260Combined sources4
Turni262 – 264Combined sources3
Beta strandi265 – 267Combined sources3
Beta strandi268 – 273Combined sources6
Turni282 – 286Combined sources5
Beta strandi290 – 294Combined sources5
Beta strandi297 – 300Combined sources4
Beta strandi305 – 311Combined sources7
Beta strandi317 – 323Combined sources7
Beta strandi326 – 329Combined sources4
Beta strandi333 – 335Combined sources3
Beta strandi338 – 343Combined sources6
Helixi345 – 355Combined sources11
Helixi359 – 362Combined sources4
Helixi365 – 374Combined sources10
Beta strandi375 – 385Combined sources11
Turni387 – 391Combined sources5
Helixi392 – 395Combined sources4
Beta strandi396 – 399Combined sources4
Beta strandi412 – 414Combined sources3
Helixi421 – 427Combined sources7
Beta strandi432 – 442Combined sources11
Turni479 – 482Combined sources4
Beta strandi483 – 489Combined sources7
Beta strandi498 – 500Combined sources3
Beta strandi502 – 506Combined sources5
Beta strandi509 – 512Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
2MWJNMR-A478-513[»]
2MWKNMR-A478-513[»]
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[»]
4D5IX-ray1.42A19-451[»]
4D5JX-ray1.50A19-451[»]
4D5OX-ray1.52A19-451[»]
4D5PX-ray1.89A19-451[»]
4D5QX-ray1.68A19-451[»]
4D5VX-ray1.62A19-451[»]
4P1HX-ray1.50A19-449[»]
4P1JX-ray2.62A19-451[»]
4UWTX-ray1.20A19-451[»]
4V0ZX-ray1.70A19-451[»]
5CELX-ray1.90A19-451[»]
5X34NMR-A478-513[»]
5X35NMR-A478-513[»]
5X36NMR-A478-513[»]
5X37NMR-A478-513[»]
5X38NMR-A478-513[»]
5X39NMR-A478-513[»]
5X3CNMR-A478-513[»]
6CELX-ray1.70A19-451[»]
7CELX-ray1.90A19-451[»]
8CELmodel-A18-451[»]
ProteinModelPortaliP62694.
SMRiP62694.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62694.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini477 – 513CBM1PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni18 – 453Catalytic1 PublicationAdd BLAST436
Regioni454 – 477LinkerCuratedAdd BLAST24

Domaini

The enzyme consists of two functional domains, a catalytic core joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-, and proline-rich, highly glycosylated linker sequence.2 Publications

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IE3Y. Eukaryota.
ENOG41101KD. LUCA.

Family and domain databases

CDDicd07999. GH7_CBH_EG. 1 hit.
Gene3Di2.70.100.10. 1 hit.
InterProiView protein in InterPro
IPR000254. Cellulose-bd_dom_fun.
IPR013320. ConA-like_dom.
IPR001722. Glyco_hydro_7.
PfamiView protein in Pfam
PF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
PRINTSiPR00734. GLHYDRLASE7.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD001821. CBD_fun. 1 hit.
SMARTiView protein in SMART
SM00236. fCBD. 1 hit.
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiView protein in PROSITE
PS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti459R → PP AA sequence (Ref. 2) Curated1

Sequence databases

PIRiA00902. EUTQI.

Similar proteinsi

Entry informationi

Entry nameiGUX1_HYPJE
AccessioniPrimary (citable) accession number: P62694
Secondary accession number(s): P00725
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: August 30, 2017
This is version 87 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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