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P38535 (XYNX_CLOTM) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Exoglucanase XynX

EC=3.2.1.91
Alternative name(s):
1,4-beta-cellobiohydrolase
Exocellobiohydrolase
Gene names
Name:xynX
OrganismClostridium thermocellum
Taxonomic identifier1515 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length1087 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Sequence similarities

Belongs to the glycosyl hydrolase 10 (cellulase F) family.

Contains 1 CBM-cenC (cenC-type cellulose-binding) domain.

Contains 3 SLH (S-layer homology) domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3030 Potential
Chain31 – 10871057Exoglucanase XynX
PRO_0000007982

Regions

Domain37 – 188152CBM-cenC
Domain903 – 96664SLH 1
Domain967 – 102559SLH 2
Domain1028 – 108760SLH 3

Sites

Active site3471Proton donor By similarity
Active site3891 By similarity
Active site4521Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
P38535 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 88077FC27AC83F51

FASTA1,087120,358
        10         20         30         40         50         60 
MKNNLSKFVS IFTAFIMIFG TSLFFPHVSA FADDNNANLV SNGDFESGTI DGWIKQGNPT 

        70         80         90        100        110        120 
LAATTEEAIG QYSMKVAGRT QTYEGPAYSF LGKMQKGQSY NVSLKVRLVS GQNSSNPLIT 

       130        140        150        160        170        180 
VTMFREDDNG KHYDTIVWQK QVSEDSWTTV NGTYTLDYTG TLKTLYMYVE SPDPTLEYYI 

       190        200        210        220        230        240 
DDVVVTPQNP IQVGEISNNQ ITIQNDIPDL SSVFKDYFPI GVAVDPSRLN DTDPHAQLTA 

       250        260        270        280        290        300 
KHFNMLVAEN AMKPESLQPT EGNFTFDNAD RIVDYAIAHN MKMRGHTLLW HNQVPDWFFQ 

       310        320        330        340        350        360 
DPSDPTKPAS RDLLLQRLKT HITTVLDHFK TKYGAQNPII GWDVVNEVLD DNGSLRNSKW 

       370        380        390        400        410        420 
LQIIGPDYIE KAFEYAHEAD PSMKLFINDY NIENNGVKTQ AMYDLVKKLK SEGVPISGIG 

       430        440        450        460        470        480 
MQMHININSN IDNIKASIEK LASLGVEIQV TELDMNMNGN VSNEALLKQA RLYKQLFDLF 

       490        500        510        520        530        540 
KAEKQYITAV VFWGVSDDVT WLSKPNAPLL FDSKLQAKPA YWAIADPSKA IPDIQSAKAL 

       550        560        570        580        590        600 
EGSPTIGANV DSSWKLVKPL YANTYVEGTV GATATVKSMW DTKNLYLLVQ VSDNTPSSND 

       610        620        630        640        650        660 
GIEIFVDKND NKSTSYETDD EHYTIKSDGT GSSDITKYVT SNADGYIVQL AIPIEDISPT 

       670        680        690        700        710        720 
LNDKIGLDVR LNDDKGSGSI DTVTVWNDYT NSQDTNTSYF GDIVLSKPAQ VATAIYGTPV 

       730        740        750        760        770        780 
IDGKIDDIWN KVDAITTNTW VLGSDGATAT AKMMWDDKYL YVLADVTDSN LNKSSVNPYE 

       790        800        810        820        830        840 
QDSVEVFVDQ NNDKTSYYES DDGQYRVNYD NEQSFGGSTN SNGFKSATSL TQSGYIVEEA 

       850        860        870        880        890        900 
IPWTSITLLN GTIIGFDLQV NDADENGKRT GIVTWCDPSG NSWQDTSGFG NLLLTGKPSG 

       910        920        930        940        950        960 
VLKKSVTFND IKDNWAKDVI EVLASRHIVE GMTDTQYEPS KTVTRAEFTA MILKLLNIKE 

       970        980        990       1000       1010       1020 
EAYNGEFSDV KNGDWYANAI EAAYKAGIIE GDGKNMRPND SITREEMTSI AMRAYEMLTS 

      1030       1040       1050       1060       1070       1080 
YKEENIGATS FNDDKSISDW AKNVVANAAK LGIINGEPSN VFAPKGIATR AEAAAIIYGL 


LEKSNNL 

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References

[1]Pack M.Y., Jung K.H.
Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M67438 Genomic DNA. Translation: AAA23227.1.
PIRS41797.

3D structure databases

ProteinModelPortalP38535.
SMRP38535. Positions 711-895.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyCBM22. Carbohydrate-Binding Module Family 22.
CBM9. Carbohydrate-Binding Module Family 9.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.60.120.260. 1 hit.
2.60.40.1190. 2 hits.
3.20.20.80. 1 hit.
InterProIPR010502. Carb-bd_dom_fam9.
IPR003305. CenC_carb-bd.
IPR008979. Galactose-bd-like.
IPR001000. Glyco_hydro_10.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR001119. S-layer_homology_dom.
[Graphical view]
PfamPF02018. CBM_4_9. 1 hit.
PF06452. DUF1083. 2 hits.
PF00331. Glyco_hydro_10. 1 hit.
PF00395. SLH. 3 hits.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMSSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
PS51272. SLH. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNX_CLOTM
AccessionPrimary (citable) accession number: P38535
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: October 16, 2013
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries