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Q8J0D2 (CBHRE_GEOS1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 41. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Oligoxyloglucan reducing end-specific cellobiohydrolase
Short name=OXG-RCBH
EC=3.2.1.150
OrganismGeotrichum sp. (strain M128)
Taxonomic identifier203496 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Dipodascaceae › mitosporic Dipodascaceae › Geotrichum

Protein attributes

Sequence length812 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

Hydrolysis of cellobiose from the reducing end of xyloglucans consisting of a beta-(1->4)-linked glucan carrying alpha-D-xylosyl groups on O-6 of the glucose residues. To be a substrate, the first residue must be unsubstituted, the second residue may bear a xylosyl group, whether further glycosylated or not, and the third residue, which becomes the new terminus by the action of the enzyme, is preferably xylosylated, but this xylose residue must not be further substituted. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 74 family. Ref.1

Contains 7 BNR repeats.

Biophysicochemical properties

pH dependence:

Optimum pH is 3.5-5.0 with the oligoxyloglucan heptasaccharide XXXG as a substrate. Over 90% activity is retained between pH 4.8 and 8.0. Ref.1

Temperature dependence:

Optimum temperature is 50-60 degrees Celsius with the oligoxyloglucan heptasaccharide XXXG as a substrate. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.1
Chain24 – 812789Oligoxyloglucan reducing end-specific cellobiohydrolase Ref.1
PRO_0000395429

Regions

Repeat118 – 12811BNR 1
Repeat218 – 22811BNR 2
Repeat350 – 36011BNR 3
Repeat595 – 60511BNR 4
Repeat637 – 64610BNR 5
Repeat681 – 69111BNR 6
Repeat736 – 74611BNR 7

Sites

Active site581Nucleophile Probable
Active site4881Proton donor Probable

Amino acid modifications

Glycosylation1801N-linked (GlcNAc...) Potential
Glycosylation2041N-linked (GlcNAc...) Potential
Glycosylation2391N-linked (GlcNAc...) Potential
Glycosylation2891N-linked (GlcNAc...) Potential
Glycosylation3121N-linked (GlcNAc...) Potential
Glycosylation5631N-linked (GlcNAc...) Potential
Glycosylation6971N-linked (GlcNAc...) Potential
Glycosylation7411N-linked (GlcNAc...) Potential
Glycosylation7541N-linked (GlcNAc...) Potential

Experimental info

Mutagenesis581D → N: No catalytic activity. Ref.2
Mutagenesis4671E → Q: No effect on catalytic activity. Ref.2
Mutagenesis4881D → N: No catalytic activity. Ref.2
Mutagenesis5131D → N: No effect on catalytic activity. Ref.2

Secondary structure

1 ............................................................................................................................................. 812
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8J0D2 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: F5C740F32D8B17E5

FASTA81287,081
        10         20         30         40         50         60 
MVAVTSLGKA LTALSILASL AVAKEHYEFK NVAIGGGGYI TGIVAHPKTK DLLYARTDIG 

        70         80         90        100        110        120 
GAYRWDAGTS KWIPLNDFIE AQDMNIMGTE SIALDPNNPD RLYLAQGRYV GDEWAAFYVS 

       130        140        150        160        170        180 
EDRGQSFTIY ESPFPMGAND MGRNNGERLA VNPFNSNEVW MGTRTEGIWK SSDRAKTWTN 

       190        200        210        220        230        240 
VTSIPDAFTN GIGYTSVIFD PERNGTIYAS ATAPQGMYVT HDGGVSWEPV AGQPSSWLNR 

       250        260        270        280        290        300 
TTGAFPDKKP ASIAPQPMKV ALTPNFLYVT YADYPGPWGV TFGEVWRQNR TSGAWDDITP 

       310        320        330        340        350        360 
RVGNSSPAPY NNQTFPAGGF CGLSVDATNP NRLVVITLDR DPGPALDSIY LSTDAGATWK 

       370        380        390        400        410        420 
DVTQLSSPSN LEGNWGHPTN AARYKDGTPV PWLDFNNGPQ WGGYGAPHGT PGLTKFGWWM 

       430        440        450        460        470        480 
SAVLIDPFNP EHLMYGTGAT IWATDTLSRV EKDWAPSWYL QIDGIEENAI LSLRSPKSGA 

       490        500        510        520        530        540 
ALLSGIGDIS GMKHDDLTKP QKMFGAPQFS NLDSIDAAGN FPNVVVRAGS SGHEYDSACA 

       550        560        570        580        590        600 
RGAYATDGGD AWTIFPTCPP GMNASHYQGS TIAVDASGSQ IVWSTKLDEQ ASGPWYSHDY 

       610        620        630        640        650        660 
GKTWSVPAGD LKAQTANVLS DKVQDGTFYA TDGGKFFVST DGGKSYAAKG AGLVTGTSLM 

       670        680        690        700        710        720 
PAVNPWVAGD VWVPVPEGGL FHSTDFGASF TRVGTANATL VSVGAPKSKS DGKKASAPSA 

       730        740        750        760        770        780 
VFIWGTDKPG SDIGLYRSDD NGSTWTRVND QEHNYSGPTM IEADPKVYGR VYLGTNGRGI 

       790        800        810 
VYADLTNKKS NEEKSTAKCA NGQKGTHCYV KK

« Hide

References

[1]"Purification, characterization, cloning, and expression of a novel xyloglucan-specific glycosidase, oligoxyloglucan reducing end-specific cellobiohydrolase."
Yaoi K., Mitsuishi Y.
J. Biol. Chem. 277:48276-48281(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-42; 51-62; 715-726 AND 767-775, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
[2]"Tandem repeat of a seven-bladed beta-propeller domain in oligoxyloglucan reducing-end-specific cellobiohydrolase."
Yaoi K., Kondo H., Noro N., Suzuki M., Tsuda S., Mitsuishi Y.
Structure 12:1209-1217(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 24-812, ACTIVE SITES, MUTAGENESIS OF ASP-58; GLU-467; ASP-488 AND ASP-513.
[3]"The structural basis for the exo-mode of action in GH74 oligoxyloglucan reducing end-specific cellobiohydrolase."
Yaoi K., Kondo H., Hiyoshi A., Noro N., Sugimoto H., Tsuda S., Mitsuishi Y., Miyazaki K.
J. Mol. Biol. 370:53-62(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 24-812 IN COMPLEX WITH HEPTAXYLOGLUCAN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB089343 mRNA. Translation: BAC22065.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SQJX-ray2.20A/B24-812[»]
2EBSX-ray2.40A/B24-812[»]
ProteinModelPortalQ8J0D2.
SMRQ8J0D2. Positions 27-809.
ModBaseSearch...

Protein family/group databases

CAZyGH74. Glycoside Hydrolase Family 74.
mycoCLAPXBH74A_GEOSP.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16634.
BRENDA3.2.1.91. 2419.

Family and domain databases

ProtoNetSearch...

Other

EvolutionaryTraceQ8J0D2.

Entry information

Entry nameCBHRE_GEOS1
AccessionPrimary (citable) accession number: Q8J0D2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 13, 2010
Last sequence update: March 1, 2003
Last modified: April 3, 2013
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents