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Protein

Endo-1,4-beta-xylanase A

Gene

xynA

Organism
Clostridium stercorarium
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Endoxylanase that degrades arabinoxylan and glucuronoxylan to xylobiose and xylotriose (in vitro).2 Publications

Catalytic activityi

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

pH dependencei

Optimum pH is 6.5-7.0.1 Publication

Temperature dependencei

Optimum temperature is 75 degrees Celsius. Thermostable.1 Publication

Pathwayi: xylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei124NucleophilePROSITE-ProRule annotation1
Active sitei214Proton donorPROSITE-ProRule annotation1
Metal bindingi253Calcium 11
Metal bindingi255Calcium 11
Binding sitei270Substrate 1; via carbonyl oxygen2 Publications1
Metal bindingi275Calcium 1; via carbonyl oxygen1
Binding sitei279Substrate 1; via amide nitrogen2 Publications1
Binding sitei336Substrate 12 Publications1
Binding sitei363Substrate 12 Publications1
Metal bindingi365Calcium 11
Metal bindingi530Calcium 21
Metal bindingi532Calcium 21
Metal bindingi552Calcium 2; via carbonyl oxygen1
Binding sitei556Substrate 2; via amide nitrogen2 Publications1
Binding sitei613Substrate 22 Publications1
Binding sitei640Substrate 22 Publications1
Metal bindingi642Calcium 21

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation, Xylan degradation

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.2.1.8. 1520.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM6. Carbohydrate-Binding Module Family 6.
GH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11B_CLOST.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase A (EC:3.2.1.8)
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Xylanase 11A
Short name:
Xyn11A
Gene namesi
Name:xynA
OrganismiClostridium stercorarium
Taxonomic identifieri1510 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000023680931 – 651Endo-1,4-beta-xylanase AAdd BLAST621

Expressioni

Inductioni

Up-regulated by growth on xylan.1 Publication

Structurei

Secondary structure

1651
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi258 – 260Combined sources3
Beta strandi266 – 269Combined sources4
Beta strandi275 – 279Combined sources5
Beta strandi285 – 292Combined sources8
Beta strandi297 – 305Combined sources9
Beta strandi310 – 318Combined sources9
Beta strandi323 – 329Combined sources7
Beta strandi339 – 348Combined sources10
Beta strandi350 – 360Combined sources11
Beta strandi363 – 371Combined sources9
Beta strandi523 – 527Combined sources5
Beta strandi535 – 538Combined sources4
Beta strandi543 – 546Combined sources4
Beta strandi550 – 555Combined sources6
Beta strandi562 – 569Combined sources8
Beta strandi574 – 582Combined sources9
Beta strandi587 – 595Combined sources9
Beta strandi600 – 606Combined sources7
Beta strandi616 – 625Combined sources10
Beta strandi627 – 637Combined sources11
Beta strandi640 – 647Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NAEX-ray2.05A507-651[»]
1O8PX-ray2.00A507-651[»]
1O8SX-ray1.15A507-651[»]
1OD3X-ray1.00A507-651[»]
1UY1X-ray1.80A235-373[»]
1UY2X-ray1.70A235-373[»]
1UY3X-ray1.89A235-373[»]
1UY4X-ray1.69A235-373[»]
ProteinModelPortaliQ8GJ44.
SMRiQ8GJ44.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8GJ44.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini33 – 227GH11PROSITE-ProRule annotationAdd BLAST195
Domaini250 – 370CBM6 1PROSITE-ProRule annotationAdd BLAST121
Repeati278 – 3391Add BLAST62
Domaini387 – 507CBM6 2PROSITE-ProRule annotationAdd BLAST121
Repeati415 – 4762Add BLAST62
Domaini527 – 647CBM6 3PROSITE-ProRule annotationAdd BLAST121
Repeati555 – 6163Add BLAST62

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni278 – 6163 X 61 AA approximate repeatsAdd BLAST339

Domaini

XynA is a modular enzyme. The number of CBM6 (carbohydrate binding type-6) domains varies between strains. The polymeric substrate can interact with several of these CBM6 domains.

Sequence similaritiesi

Contains 3 CBM6 (carbohydrate binding type-6) domains.PROSITE-ProRule annotation
Contains 1 GH11 (glycosyl hydrolase family 11) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
2.60.120.260. 3 hits.
InterProiIPR006584. Cellulose-bd_IV.
IPR005084. CMB_fam6.
IPR013320. ConA-like_dom.
IPR008979. Galactose-bd-like.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR001137. Glyco_hydro_11.
[Graphical view]
PfamiPF03422. CBM_6. 3 hits.
PF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SMARTiSM00606. CBD_IV. 3 hits.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 3 hits.
SSF49899. SSF49899. 1 hit.
PROSITEiPS51175. CBM6. 3 hits.
PS00776. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8GJ44-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRKVKKMAA MATSIIMAIM IILHSIPVLA GRIIYDNETG THGGYDYELW
60 70 80 90 100
KDYGNTIMEL NDGGTFSCQW SNIGNALFRK GRKFNSDKTY QELGDIVVEY
110 120 130 140 150
GCDYNPNGNS YLCVYGWTRN PLVEYYIVES WGSWRPPGAT PKGTITVDGG
160 170 180 190 200
TYEIYETTRV NQPSIDGTAT FQQYWSVRTS KRTSGTISVT EHFKQWERMG
210 220 230 240 250
MRMGKMYEVA LTVEGYQSSG YANVYKNEIR IGANPTPAPS QSPIRRDAFS
260 270 280 290 300
IIEAEEYNST NSSTLQVIGT PNNGRGIGYI ENGNTVTYSN IDFGSGATGF
310 320 330 340 350
SATVATEVNT SIQIRSDSPT GTLLGTLYVS STGSWNTYQT VSTNISKITG
360 370 380 390 400
VHDIVLVFSG PVNVDNFIFS RSSPVPAPGD NTRDAYSIIQ AEDYDSSYGP
410 420 430 440 450
NLQIFSLPGG GSAIGYIENG YSTTYNNVNF ANGLSSITAR VATQISTSIQ
460 470 480 490 500
VRAGGATGTL LGTIYVPSTN SWDSYQNVTA NLSNITGVHD ITLVFSGPVN
510 520 530 540 550
VDYFVFTPAN VNSGPTSPVG GTRSAFSNIQ AEDYDSSYGP NLQIFSLPGG
560 570 580 590 600
GSAIGYIENG YSTTYKNIDF GDGATSVTAR VATQNATTIQ VRLGSPSGTL
610 620 630 640 650
LGTIYVGSTG SFDTYRDVSA TISNTAGVKD IVLVFSGPVN VDWFVFSKSG

T
Length:651
Mass (Da):70,151
Last modified:May 30, 2006 - v2
Checksum:i52E501A16F9D1423
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti649 – 651SGT → FRNLRV in CAD48307 (PubMed:15256568).Curated3

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ508403 Genomic DNA. Translation: CAD48307.1.
AF417638 Genomic DNA. Translation: AAL14106.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ508403 Genomic DNA. Translation: CAD48307.1.
AF417638 Genomic DNA. Translation: AAL14106.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NAEX-ray2.05A507-651[»]
1O8PX-ray2.00A507-651[»]
1O8SX-ray1.15A507-651[»]
1OD3X-ray1.00A507-651[»]
1UY1X-ray1.80A235-373[»]
1UY2X-ray1.70A235-373[»]
1UY3X-ray1.89A235-373[»]
1UY4X-ray1.69A235-373[»]
ProteinModelPortaliQ8GJ44.
SMRiQ8GJ44.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM6. Carbohydrate-Binding Module Family 6.
GH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11B_CLOST.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.
BRENDAi3.2.1.8. 1520.

Miscellaneous databases

EvolutionaryTraceiQ8GJ44.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
2.60.120.260. 3 hits.
InterProiIPR006584. Cellulose-bd_IV.
IPR005084. CMB_fam6.
IPR013320. ConA-like_dom.
IPR008979. Galactose-bd-like.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR001137. Glyco_hydro_11.
[Graphical view]
PfamiPF03422. CBM_6. 3 hits.
PF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SMARTiSM00606. CBD_IV. 3 hits.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 3 hits.
SSF49899. SSF49899. 1 hit.
PROSITEiPS51175. CBM6. 3 hits.
PS00776. GH11_1. 1 hit.
PS00777. GH11_2. 1 hit.
PS51761. GH11_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXYNA1_CLOSR
AccessioniPrimary (citable) accession number: Q8GJ44
Secondary accession number(s): Q93AQ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: May 30, 2006
Last modified: November 2, 2016
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.