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O69230 (XYNC_PAEBA) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Endo-1,4-beta-xylanase C

Short name=Xylanase C
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase C
Gene names
Name:xynC
OrganismPaenibacillus barcinonensis
Taxonomic identifier198119 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

Protein attributes

Sequence length1086 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endoxylanase with high hydrolytic activity on birchwood and oat spelt xylan. Xylotetraose, xylotriose, xylobiose and xylose are the main products from birchwood xylan hydrolysis. Shows increasing activity on xylo-oligosaccharides of increasing length. Displays very low hydrolytic activity on Avicel, carboxymethylcellulose (CMC) and p-nitrophenyl-beta-xylopyranoside. Also shows transxylosidase activity, allowing the formation of xylo-oligosaccharides of higher degreee of polymerization than the starting substrate. Ref.1

Catalytic activity

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans. Ref.1

Pathway

Glycan degradation; xylan degradation.

Domain

Consists of three different domains. The central region of the enzyme is the catalytic domain. The N-terminal region contains cenC-type cellulose-binding domains and seems to act as a thermostabilizing domain: a derivative lacking this region shows a lower optimum temperature for activity (35 degrees Celsius) than the full-length enzyme, and a reduced thermal stability that results in a complete inactivation of the enzyme after 2 hours incubation at 55 degrees Celsius. The C-terminal region contains family 9 carbohydrate-binding modules.

Sequence similarities

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

Contains 2 CBM-cenC (cenC-type cellulose-binding) domains.

Biophysicochemical properties

pH dependence:

Optimum pH is 5. Retains at least 50% of its maximum activity between pH 4.5 and 8.0. Is not active at pH values below 4.5, while at least 35% of maximum activity is found in the pH range 8.5-11.0. Ref.1

Temperature dependence:

Optimum temperature is 45 degrees Celsius. Is only stable at 55 degrees Celsius or lower temperatures. Retains more than 77% activity after 2 hours incubation at 55 degrees Celsius and pH 7.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
Gene Ontology (GO)
   Biological_processxylan catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

endo-1,4-beta-xylanase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 10861055Endo-1,4-beta-xylanase C
PRO_0000371420

Regions

Domain35 – 183149CBM-cenC 1
Domain197 – 359163CBM-cenC 2
Region370 – 711342Catalytic

Sites

Active site5021Proton donor By similarity
Active site5561 By similarity
Active site6201Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
O69230 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 4378361F1801A326

FASTA1,086120,586
        10         20         30         40         50         60 
MRGKWLRLCL AAVLIVSLLP GLGAGEWKAS AAKAGDILLS HSFEEGTTQG WTARGGVKVD 

        70         80         90        100        110        120 
VTAEQAYQGK QSLQTTGRTE AWNGPSLSLT DVVHKNEVVE ISGYVKLVAG SAPPDLKFTV 

       130        140        150        160        170        180 
ERRDRNGDTQ YDQVNAAEQV TDQKWVKLQG QYSYEQGSSL LLYLESTDAK AAYLLDEFQI 

       190        200        210        220        230        240 
RLVKAAPENP GEPGEAGQAL FKAYFEDGNI GNWRARGTEK LEVVSGIGHN SNRSLKTSSR 

       250        260        270        280        290        300 
SETYHGPLVE VLPYLQKGST VHISFWAMYD EGPATQVING SLEKEFNRDT ANLEYAMFAS 

       310        320        330        340        350        360 
TTLNKGQWKK IEADIIVPAE STGISGLRMY AETPWKQSSE VTETDTIPFY VDDVQITATE 

       370        380        390        400        410        420 
AIAIEKNIPD LAKKLGSSYA LGAAIDQTAL DPKDPHSELL TKHFNSITAG NFMKMDAMQP 

       430        440        450        460        470        480 
TEGKFVWSEA DKLVNFAAAN NMQVRGHTLL WHSQVPDWFF TDPNDPSKPA TREQLMQRMK 

       490        500        510        520        530        540 
THIQTIVSRY KGKVHTWDVV NEVISDGGGL RNQASGSKWR DIIGDVDGDG DDSDYIELAF 

       550        560        570        580        590        600 
RYAREADPDA VLVINDYGIE GSVSKMNDMV KLVEKLLAKG TPIDAIGFQM HVSMYGPDIK 

       610        620        630        640        650        660 
QIREAFNRAA ALGVHIQVTE LDMSIYSGNS EQEKPVTDEM MLEQAYRYRA LFDLFKEFDD 

       670        680        690        700        710        720 
RGVMDSVTLW GLADDGTWLD DFPVKGRKDA PLLFDRKLKA KPAYWALVDP STLPVYRNEW 

       730        740        750        760        770        780 
TASQAKVSLP DRKGQEDIIW GAVRALPFSH VIEGAVGTTG EVKTLWDGKQ LNLRIEVKDA 

       790        800        810        820        830        840 
TRLKGDQVEV FVSPEDMTAG KKNSTPKDGQ YIFNRDGGKG KDQKLYQVKE NKSGYVVYAS 

       850        860        870        880        890        900 
LPLSSADLAA GKVLSLDFRI TDKQPNGKTS IVVWNDVNNQ QPQKTENRGK LKLGFDLKHA 

       910        920        930        940        950        960 
KVMYGTPTVD GKEDKLWKKA VTITTDVKVT GNSGAKAKAK LLWDEKYLYV LAEVKDPLLS 

       970        980        990       1000       1010       1020 
KKSANAHEQD SIELFIDLNK NQTNSYEEDD AQYRVNFDNE TSFGGSPRKE LFKSATRLTK 

      1030       1040       1050       1060       1070       1080 
EGYIVEAAIP LENVRTKESK WIGFDLQVND DGAGDGKRSS VFMWSDPSGN SYRDTSGFGS 


LLLMKK 

« Hide

References

[1]"A multidomain xylanase from a Bacillus sp. with a region homologous to thermostabilizing domains of thermophilic enzymes."
Blanco A., Diaz P., Zueco J., Parascandola P., Pastor F.I.J.
Microbiology 145:2163-2170(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: DSM 15478 / CECT 7022 / BP-23.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ006645 Genomic DNA. Translation: CAA07173.1.
PIRT17628.

3D structure databases

ProteinModelPortalO69230.
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...

Enzyme and pathway databases

UniPathwayUPA00114.

Family and domain databases

Gene3D2.60.120.260. 2 hits.
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.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF02018. CBM_4_9. 2 hits.
PF06452. DUF1083. 2 hits.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSPR00134. GLHYDRLASE10.
SMARTSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMSSF49785. SSF49785. 2 hits.
SSF51445. SSF51445. 1 hit.
PROSITEPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNC_PAEBA
AccessionPrimary (citable) accession number: O69230
Entry history
Integrated into UniProtKB/Swiss-Prot: May 5, 2009
Last sequence update: August 1, 1998
Last modified: November 13, 2013
This is version 75 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries