Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q8GJ44

- XYNA1_CLOSR

UniProt

Q8GJ44 - XYNA1_CLOSR

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
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 2 (30 May 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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-SubCell

    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 – 2603
    Beta strandi266 – 2694
    Beta strandi275 – 2795
    Beta strandi285 – 2928
    Beta strandi297 – 3059
    Beta strandi310 – 3189
    Beta strandi323 – 3297
    Beta strandi339 – 34810
    Beta strandi350 – 36011
    Beta strandi363 – 3719
    Beta strandi523 – 5275
    Beta strandi535 – 5384
    Beta strandi543 – 5464
    Beta strandi550 – 5556
    Beta strandi562 – 5698
    Beta strandi574 – 5829
    Beta strandi587 – 5959
    Beta strandi600 – 6067
    Beta strandi616 – 62510
    Beta strandi627 – 63711
    Beta strandi640 – 6478

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    IPR008985. ConA-like_lec_gl_sf.
    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

    MKRKVKKMAA MATSIIMAIM IILHSIPVLA GRIIYDNETG THGGYDYELW    50
    KDYGNTIMEL NDGGTFSCQW SNIGNALFRK GRKFNSDKTY QELGDIVVEY 100
    GCDYNPNGNS YLCVYGWTRN PLVEYYIVES WGSWRPPGAT PKGTITVDGG 150
    TYEIYETTRV NQPSIDGTAT FQQYWSVRTS KRTSGTISVT EHFKQWERMG 200
    MRMGKMYEVA LTVEGYQSSG YANVYKNEIR IGANPTPAPS QSPIRRDAFS 250
    IIEAEEYNST NSSTLQVIGT PNNGRGIGYI ENGNTVTYSN IDFGSGATGF 300
    SATVATEVNT SIQIRSDSPT GTLLGTLYVS STGSWNTYQT VSTNISKITG 350
    VHDIVLVFSG PVNVDNFIFS RSSPVPAPGD NTRDAYSIIQ AEDYDSSYGP 400
    NLQIFSLPGG GSAIGYIENG YSTTYNNVNF ANGLSSITAR VATQISTSIQ 450
    VRAGGATGTL LGTIYVPSTN SWDSYQNVTA NLSNITGVHD ITLVFSGPVN 500
    VDYFVFTPAN VNSGPTSPVG GTRSAFSNIQ AEDYDSSYGP NLQIFSLPGG 550
    GSAIGYIENG YSTTYKNIDF GDGATSVTAR VATQNATTIQ VRLGSPSGTL 600
    LGTIYVGSTG SFDTYRDVSA TISNTAGVKD IVLVFSGPVN VDWFVFSKSG 650
    T 651
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ508403 Genomic DNA. Translation: CAD48307.1.
    AF417638 Genomic DNA. Translation: AAL14106.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ508403 Genomic DNA. Translation: CAD48307.1 .
    AF417638 Genomic DNA. Translation: AAL14106.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    IPR008985. ConA-like_lec_gl_sf.
    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: October 1, 2014
    This is version 69 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