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P33558

- XYNA2_CLOSR

UniProt

P33558 - XYNA2_CLOSR

Protein

Endo-1,4-beta-xylanase A

Gene

xynA

Organism
Clostridium stercorarium
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Temperature dependencei

    Optimum temperature is 70 degrees Celsius. Thermostable.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei124 – 1241NucleophilePROSITE-ProRule annotation
    Active sitei215 – 2151Proton donorPROSITE-ProRule annotation
    Metal bindingi254 – 2541Calcium 1By similarity
    Metal bindingi256 – 2561Calcium 1By similarity
    Binding sitei271 – 2711Substrate 1; via carbonyl oxygenBy similarity
    Metal bindingi276 – 2761Calcium 1; via carbonyl oxygenBy similarity
    Binding sitei280 – 2801Substrate 1; via amide nitrogenBy similarity
    Binding sitei337 – 3371Substrate 1By similarity
    Binding sitei364 – 3641Substrate 1By similarity
    Metal bindingi366 – 3661Calcium 1By similarity
    Metal bindingi391 – 3911Calcium 2By similarity
    Metal bindingi393 – 3931Calcium 2By similarity
    Metal bindingi413 – 4131Calcium 2; via carbonyl oxygenBy similarity
    Binding sitei417 – 4171Substrate 2; via amide nitrogenBy similarity
    Binding sitei474 – 4741Substrate 2By similarity
    Binding sitei501 – 5011Substrate 2By similarity
    Metal bindingi503 – 5031Calcium 2By similarity

    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

    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)
    Short name:
    Xylanase A
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase A
    Gene namesi
    Name:xynA
    OrganismiClostridium stercorarium
    Taxonomic identifieri1510 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 512482Endo-1,4-beta-xylanase APRO_0000008002Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliP33558.
    SMRiP33558. Positions 33-374, 379-509.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini251 – 371121CBM6 1PROSITE-ProRule annotationAdd
    BLAST
    Repeati279 – 340621Add
    BLAST
    Domaini388 – 508121CBM6 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati416 – 477622Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni279 – 4771992 X 61 AA approximate repeatsAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi236 – 2449Pro-rich

    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 By similarity.By similarity

    Sequence similaritiesi

    Contains 2 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. 2 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. 2 hits.
    PF00457. Glyco_hydro_11. 1 hit.
    [Graphical view]
    PRINTSiPR00911. GLHYDRLASE11.
    SMARTiSM00606. CBD_IV. 2 hits.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 2 hits.
    SSF49899. SSF49899. 1 hit.
    PROSITEiPS51175. CBM6. 2 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.

    P33558-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRKVKKMAA MATSIIMAIM IILHSIPVLA GRIIYDNETG THGGYDYELW    50
    KDYGNTIMEL NDGGTFSCQW SNIGNALFRK GRKFNSDKTY QELGDIVVEY 100
    GCDYNPNGNS YLCVYGWTRN PLVEYYIVES WGSWRPPGAT PKGTITQWMA 150
    GTYEIYETTR VNQPSIDGTA TFQQYWSVRT SKRTSGTISV TEHFKQWERM 200
    GMRMGKMYEV ALTVEGYQSS GYANVYKNEI RIGANPTPAP SQSPIRRDAF 250
    SIIEAEEYNS TNSSTLQVIG TPNNGRGIGY IENGNTVTYS NIDFGSGATG 300
    FSATVATEVN TSIQIRSDSP TGTLLGTLYV SSTGSWNTYQ TVSTNISKIT 350
    GVHDIVLVFS GPVNVDNFIF SRSSPVPAPG DNTRDAYSII QAEDYDSSYG 400
    PNLQIFSLPG GGSAIGYIEN GYSTTYKNID FGDGATSVTA RVATQNATTI 450
    QVRLGSPSGT LLGTIYVGST GSFDTYRDVS ATISNTAGVK DIVLVFSGPV 500
    NVDWFVFSKS GT 512
    Length:512
    Mass (Da):55,843
    Last modified:February 1, 1996 - v2
    Checksum:i1E133CBF4C139305
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13325 Genomic DNA. Translation: BAA02584.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13325 Genomic DNA. Translation: BAA02584.1 .

    3D structure databases

    ProteinModelPortali P33558.
    SMRi P33558. Positions 33-374, 379-509.
    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 .

    Family and domain databases

    Gene3Di 2.60.120.180. 1 hit.
    2.60.120.260. 2 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. 2 hits.
    PF00457. Glyco_hydro_11. 1 hit.
    [Graphical view ]
    PRINTSi PR00911. GLHYDRLASE11.
    SMARTi SM00606. CBD_IV. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49785. SSF49785. 2 hits.
    SSF49899. SSF49899. 1 hit.
    PROSITEi PS51175. CBM6. 2 hits.
    PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
    PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the Clostridium stercorarium xynA gene encoding xylanase A: identification of catalytic and cellulose binding domains."
      Sakka K., Kojima Y., Kondo T., Karita S., Ohmiya K., Shimada K.
      Biosci. Biotechnol. Biochem. 57:273-277(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-40.
      Strain: F-9.
    2. Sakka K.
      Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.

    Entry informationi

    Entry nameiXYNA2_CLOSR
    AccessioniPrimary (citable) accession number: P33558
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 94 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

    Direct protein sequencing

    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