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P36917 (XYNA_THESA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 92. 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 A

Short name=Xylanase A
EC=3.2.1.8
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Gene names
Name:xynA
OrganismThermoanaerobacterium saccharolyticum
Taxonomic identifier28896 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisThermoanaerobacterium

Protein attributes

Sequence length1157 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Endo-acting enzyme that randomly cleaves the internal xylosidic linkages of the xylan backbone, yielding xylooligosaccharides of various lengths which are further hydrolyzed to xylose molecules by beta-xylosidase (EC 3.2.1.37). Requires at least three xylose residues for catalytic activity. Does not have activity against xylobiose.

Catalytic activity

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

Pathway

Glycan degradation; xylan degradation.

Induction

By xylan and xylose.

Sequence similarities

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

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

Contains 2 SLH (S-layer homology) domains.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5.

Temperature dependence:

Optimum temperature is 70 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Polysaccharide degradation
Xylan degradation
   DomainRepeat
Signal
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
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 – 3333 Ref.1
Chain34 – 11571124Endo-1,4-beta-xylanase A
PRO_0000007980

Regions

Domain38 – 189152CBM-cenC 1
Domain195 – 343149CBM-cenC 2
Domain1051 – 111464SLH 1
Domain1115 – 115743SLH 2
Region413 – 649237Catalytic Potential

Sites

Active site4951Proton donor By similarity
Active site5371 Ref.2
Active site6001Nucleophile Ref.2

Experimental info

Mutagenesis5371D → N: Loss of activity.
Mutagenesis6001E → Q: Loss of activity.
Mutagenesis6021D → N: Loss of activity.

Sequences

Sequence LengthMass (Da)Tools
P36917 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 51FA6004497EC58B

FASTA1,157128,380
        10         20         30         40         50         60 
MMKNNVDRIV SIVTALIMIF GASLFSPPIR VFADDTNINL VSNGDFESGT IDGWIKQGNP 

        70         80         90        100        110        120 
TLAVTTEQAI GQYSMKVTGR TQTYEGPAYS FLGKMQKGES YSVSLKVRLV SGQNSSNPLI 

       130        140        150        160        170        180 
TVTMFREDDN GKHYDTIVWQ KQVSEDSWTT VSGTYTLDYI GTLKTLYMYV ESPDPTLEYY 

       190        200        210        220        230        240 
IDDVVVTTQN PIQVGNVIAN ETFENGNTSG WIGTGSSVVK AVYGVAHSGD YSLLTTGRTA 

       250        260        270        280        290        300 
NWNGPSYDLT GKIVPGQQYN VDFWVKFVNG NDTEQIKATV KATSDKDNYI QVNDFANVNK 

       310        320        330        340        350        360 
GEWTEIKGSF TLPVADYSGI SIYVESQNPT LEFYIDDFSV IGEISNNQIT IQNDIPDLYS 

       370        380        390        400        410        420 
VFKDYFPIGV AVDPSRLNDA DPHAQLTAKH FNMLVAENAM KPESLQPTEG NFTFDNADKI 

       430        440        450        460        470        480 
VDYAIAHNMK MRGHTLLWHN QVPDWFFQDP SDPSKSASRD LLLQRLKTHI TTVLDHFKTK 

       490        500        510        520        530        540 
YGSQNPIIGW DVVNEVLDDN GNLRNSKWLQ IIGPDYIEKA FEYAHEADPS MKLFINDYNI 

       550        560        570        580        590        600 
ENNGVKTQAM YDLVKKLKSE GVPIDGIGMQ MHININSNID NIKASIEKLA SLGVEIQVTE 

       610        620        630        640        650        660 
LDMNMNGNIS NEALLKQARL YKQLFDLFKA EKQYITAVVF WGVSDDVTWL SKPNAPLLFD 

       670        680        690        700        710        720 
SKLQAKPAFW AVVDPSKAIP DIQSAKALEG SPTIGANVDS SWKLVKPLYV NTYVEGTVGA 

       730        740        750        760        770        780 
TATVKSMWDT KNLYLLVQVS DNTPSNNDGI EIFVDKNDDK STSYETDDER YTIKRDGTGS 

       790        800        810        820        830        840 
SDITKYVTSN ADGYVAQLAI PIEDISPAVN DKIGFDIRIN DDKGNGKIDA ITVWNDYTNS 

       850        860        870        880        890        900 
QNTNTSYFGD IVLSKSAQIA TAIYGTPVID GKVDDIWNNV EPISTNTWIL GSNGATATQK 

       910        920        930        940        950        960 
MMWDDKYLYV LADVTDSNLN KSSINPYEQD SVEVFVDQNN DKTTYYENDD GQYRVNYDNE 

       970        980        990       1000       1010       1020 
QSFGGSTNSN GFKSATSLTQ SGYIVEEAIP WTSITPSNGT IIGFDLQVNN ADENGKRTGI 

      1030       1040       1050       1060       1070       1080 
VTWCDPSGNS WQDTSGFGNL LLTGKPSGAL KKGVTFDDIK NSWAKDAIEV LASRHIVEGM 

      1090       1100       1110       1120       1130       1140 
TDTQYEPNKT VTRAEFTAMI LRLLNIKEEQ YSGEFSDVNS GDWYANAIEA AYKAGIIEGD 

      1150 
GKNARPNDSI TREEMTQ 

« Hide

References

[1]"Gene cloning, sequencing, and biochemical characterization of endoxylanase from Thermoanaerobacterium saccharolyticum B6A-RI."
Lee Y.-E., Lowe S.E., Zeikus J.G.
Appl. Environ. Microbiol. 59:3134-3137(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-41.
Strain: ATCC 49915 / DSM 7060 / B6A-RI.
[2]"Characterization of the active site and thermostability regions of endoxylanase from Thermoanaerobacterium saccharolyticum B6A-RI."
Lee Y.-E., Lowe S.E., Henrissat B., Zeikus J.G.
J. Bacteriol. 175:5890-5898(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: ACTIVE SITE, MUTAGENESIS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97882 Genomic DNA. Translation: AAA21812.1. Sequence problems.
PIRA48490.

3D structure databases

ProteinModelPortalP36917.
SMRP36917. Positions 859-1043.
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.
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. 2 hits.
PF06452. DUF1083. 2 hits.
PF00331. Glyco_hydro_10. 1 hit.
PF00395. SLH. 2 hits.
[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.
PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
PS51272. SLH. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameXYNA_THESA
AccessionPrimary (citable) accession number: P36917
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: January 22, 2014
This is version 92 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