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Q8GJ44

- XYNA1_CLOSR

UniProt

Q8GJ44 - XYNA1_CLOSR

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Protein

Endo-1,4-beta-xylanase A

Gene

xynA

Organism
Clostridium stercorarium
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei124 – 1241NucleophilePROSITE-ProRule annotation
Active sitei214 – 2141Proton donorPROSITE-ProRule annotation
Metal bindingi253 – 2531Calcium 1
Metal bindingi255 – 2551Calcium 1
Binding sitei270 – 2701Substrate 1; via carbonyl oxygen2 Publications
Metal bindingi275 – 2751Calcium 1; via carbonyl oxygen
Binding sitei279 – 2791Substrate 1; via amide nitrogen2 Publications
Binding sitei336 – 3361Substrate 12 Publications
Binding sitei363 – 3631Substrate 12 Publications
Metal bindingi365 – 3651Calcium 1
Metal bindingi530 – 5301Calcium 2
Metal bindingi532 – 5321Calcium 2
Metal bindingi552 – 5521Calcium 2; via carbonyl oxygen
Binding sitei556 – 5561Substrate 2; via amide nitrogen2 Publications
Binding sitei613 – 6131Substrate 22 Publications
Binding sitei640 – 6401Substrate 22 Publications
Metal bindingi642 – 6421Calcium 2

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. endo-1,4-beta-xylanase activity Source: UniProtKB-EC
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
  2. xylan catabolic process Source: UniProtKB-UniPathway
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.

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

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 651621Endo-1,4-beta-xylanase APRO_0000236809Add
BLAST

Expressioni

Inductioni

Up-regulated by growth on xylan.1 Publication

Structurei

Secondary structure

1
651
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi258 – 2603Combined sources
Beta strandi266 – 2694Combined sources
Beta strandi275 – 2795Combined sources
Beta strandi285 – 2928Combined sources
Beta strandi297 – 3059Combined sources
Beta strandi310 – 3189Combined sources
Beta strandi323 – 3297Combined sources
Beta strandi339 – 34810Combined sources
Beta strandi350 – 36011Combined sources
Beta strandi363 – 3719Combined sources
Beta strandi523 – 5275Combined sources
Beta strandi535 – 5384Combined sources
Beta strandi543 – 5464Combined sources
Beta strandi550 – 5556Combined sources
Beta strandi562 – 5698Combined sources
Beta strandi574 – 5829Combined sources
Beta strandi587 – 5959Combined sources
Beta strandi600 – 6067Combined sources
Beta strandi616 – 62510Combined sources
Beta strandi627 – 63711Combined sources
Beta strandi640 – 6478Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 33-373, 378-507, 518-648.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8GJ44.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini250 – 370121CBM6 1PROSITE-ProRule annotationAdd
BLAST
Repeati278 – 339621Add
BLAST
Domaini387 – 507121CBM6 2PROSITE-ProRule annotationAdd
BLAST
Repeati415 – 476622Add
BLAST
Domaini527 – 647121CBM6 3PROSITE-ProRule annotationAdd
BLAST
Repeati555 – 616623Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni278 – 6163393 X 61 AA approximate repeatsAdd
BLAST

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

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.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[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. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti649 – 6513SGT → FRNLRV in CAD48307. (PubMed:15256568)Curated

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
Entry Method Resolution (Å) Chain Positions PDBsum
1NAE X-ray 2.05 A 507-651 [» ]
1O8P X-ray 2.00 A 507-651 [» ]
1O8S X-ray 1.15 A 507-651 [» ]
1OD3 X-ray 1.00 A 507-651 [» ]
1UY1 X-ray 1.80 A 235-373 [» ]
1UY2 X-ray 1.70 A 235-373 [» ]
1UY3 X-ray 1.89 A 235-373 [» ]
1UY4 X-ray 1.69 A 235-373 [» ]
ProteinModelPortali Q8GJ44.
SMRi Q8GJ44. Positions 33-373, 378-507, 518-648.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM6. Carbohydrate-Binding Module Family 6.
GH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00114 .
BRENDAi 3.2.1.8. 1520.

Miscellaneous databases

EvolutionaryTracei Q8GJ44.

Family and domain databases

Gene3Di 2.60.120.180. 1 hit.
2.60.120.260. 3 hits.
InterProi IPR006584. Cellulose-bd_IV.
IPR005084. CMB_fam6.
IPR013320. ConA-like_dom.
IPR008979. Galactose-bd-like.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view ]
Pfami PF03422. CBM_6. 3 hits.
PF00457. Glyco_hydro_11. 1 hit.
[Graphical view ]
PRINTSi PR00911. GLHYDRLASE11.
SMARTi SM00606. CBD_IV. 3 hits.
[Graphical view ]
SUPFAMi SSF49785. SSF49785. 3 hits.
SSF49899. SSF49899. 1 hit.
PROSITEi PS51175. CBM6. 3 hits.
PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Enzyme system of Clostridium stercorarium for hydrolysis of arabinoxylan: reconstitution of the in vivo system from recombinant enzymes."
    Adelsberger H., Hertel C., Glawischnig E., Zverlov V.V., Schwarz W.H.
    Microbiology 150:2257-2266(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: NCIB 11745.
  2. "Co-operative binding of triplicate carbohydrate-binding modules from a thermophilic xylanase."
    Boraston A.B., McLean B.W., Chen G., Li A., Warren R.A.J., Kilburn D.G.
    Mol. Microbiol. 43:187-194(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 235-651, FUNCTION.
    Strain: NCIB 11745.
  3. "Structure and ligand binding of carbohydrate-binding module CsCBM6-3 reveals similarities with fucose-specific lectins and 'galactose-binding' domains."
    Boraston A.B., Notenboom V., Warren R.A.J., Kilburn D.G., Rose D.R., Davies G.
    J. Mol. Biol. 327:659-669(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) OF 507-651 IN COMPLEX WITH SUBSTRATE AND CALCIUM IONS.
  4. "Binding sub-site dissection of a family 6 carbohydrate-binding module by X-ray crystallography and isothermal titration."
    Van Bueren A.L., Boraston A.B.
    Submitted (JUN-2004) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 235-373 IN COMPLEX WITH SUBSTRATE AND CALCIUM IONS.

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 26, 2014
This is version 71 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

External Data

Dasty 3