Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Endo-1,4-beta-xylanase A

Gene

xynA

Organism
Caldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

pH dependencei

Optimum pH is 5.5-6.0.

Temperature dependencei

Optimum temperature is 70 degrees Celsius.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei144 – 1441Proton donorBy similarity
Active sitei252 – 2521NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

  1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH10. Glycoside Hydrolase Family 10.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase A (EC:3.2.1.8)
Short name:
Xylanase A
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Gene namesi
Name:xynA
OrganismiCaldicellulosiruptor saccharolyticus (Caldocellum saccharolyticum)
Taxonomic identifieri44001 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 342342Endo-1,4-beta-xylanase APRO_0000007984Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP23556.
SMRiP23556. Positions 16-341.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P23556-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRCLIVCENL EMLNLSLAKT YKDYFKIGAA VTAKDLEGVH RDILLKHFNS
60 70 80 90 100
LTPENAMKFE NIHPEEQRYN FEEVARIKEF AIKNDMKLRG HTFVWHNQTP
110 120 130 140 150
GWVFLDKNGE EASKELVIER LREHIKTLCE RYKDVVYAWD VVNEAVEDKT
160 170 180 190 200
EKLLRESNWR KIIGDDYIKI AFEIAREYAG DAKLFYNDYN NEMPYKLEKT
210 220 230 240 250
YKVLKELLER GTPIDGIGIQ AHWNIWDKNL VSNLKKAIEV YASLGLEIHI
260 270 280 290 300
TELDISVFEF EDKRTDLFEP TPEMLELQAK VYEDVFAVFR EYKDVITSVT
310 320 330 340
LWGISDRHTW KDNFPVKGRK DWPLLFDVNG KPKEALYRIL RF
Length:342
Mass (Da):40,455
Last modified:November 1, 1991 - v1
Checksum:iC5380F2AB0CC0271
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34459 Genomic DNA. Translation: AAA23059.1.
AF005383 Genomic DNA. Translation: AAB87374.1.
PIRiA37202. A60154.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34459 Genomic DNA. Translation: AAA23059.1.
AF005383 Genomic DNA. Translation: AAB87374.1.
PIRiA37202. A60154.

3D structure databases

ProteinModelPortaliP23556.
SMRiP23556. Positions 16-341.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequence analysis, and expression of genes encoding xylan-degrading enzymes from the thermophile 'Caldocellum saccharolyticum'."
    Luethi E., Love D.R., McAnulty J., Wallace C., Caughey P.A., Saul D.J., Bergquist P.L.
    Appl. Environ. Microbiol. 56:1017-1024(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "A cluster of genes involved in xylan degradation cloned from the extreme thermophile Caldicellulosiruptor saccharolyticus."
    Te'O V.S. Jr., Gibbs M.D., Saul D.J., Bergquist P.L.
    Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Xylanase from the extremely thermophilic bacterium 'Caldocellum saccharolyticum': overexpression of the gene in Escherichia coli and characterization of the gene product."
    Luethi E., Jasmat N.B., Bergquist P.L.
    Appl. Environ. Microbiol. 56:2677-2683(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.

Entry informationi

Entry nameiXYNA_CALSA
AccessioniPrimary (citable) accession number: P23556
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: January 7, 2015
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.