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)

P17137

- XYNA_CLOSA

UniProt

P17137 - XYNA_CLOSA

Protein

Endo-1,4-beta-xylanase

Gene

xynB

Organism
Clostridium saccharobutylicum
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 79 (01 Oct 2014)
      Sequence version 1 (01 Aug 1990)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei152 – 1521NucleophilePROSITE-ProRule annotation
    Active sitei242 – 2421Proton donorPROSITE-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

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    UniPathwayiUPA00114.

    Protein family/group databases

    CAZyiGH11. Glycoside Hydrolase Family 11.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-1,4-beta-xylanase (EC:3.2.1.8)
    Short name:
    Xylanase
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase
    Gene namesi
    Name:xynB
    OrganismiClostridium saccharobutylicum
    Taxonomic identifieri169679 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Add
    BLAST
    Chaini29 – 261233Endo-1,4-beta-xylanasePRO_0000008001Add
    BLAST

    Proteomic databases

    PRIDEiP17137.

    Structurei

    3D structure databases

    ProteinModelPortaliP17137.
    SMRiP17137. Positions 60-259.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.60.120.180. 1 hit.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR001137. Glyco_hydro_11.
    IPR013319. Glyco_hydro_11/12.
    IPR018208. Glyco_hydro_11_AS.
    [Graphical view]
    PfamiPF00457. Glyco_hydro_11. 1 hit.
    [Graphical view]
    PRINTSiPR00911. GLHYDRLASE11.
    SUPFAMiSSF49899. SSF49899. 1 hit.
    PROSITEiPS00776. 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.

    P17137-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRRKVIFTV LATLVMTSLT IVDNTAFAAT NLNTTESTFS KEVLSTQKTY    50
    SAFNTQAAPK TITSNEIGVN GGYDYELWKD YGNTSMTLKN GGAFSCQWSN 100
    IGNALFRKGK KFNDTQTYKQ LGNISVNYDC NYQPYGNSYL CVYGWTSSPL 150
    VEYYIVDSWG SWRPPGGTSK GTITVDGGIY DIYETTRINQ PSIQGNTTFK 200
    QYWSVRRTKR TSGTISVSKH FAAWESKGMP LGKMHETAFN IEGYQSSGKA 250
    DVNSMSINIG K 261
    Length:261
    Mass (Da):29,033
    Last modified:August 1, 1990 - v1
    Checksum:i339C3616F6FD14AE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31726 Genomic DNA. Translation: AAA23287.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31726 Genomic DNA. Translation: AAA23287.1 .

    3D structure databases

    ProteinModelPortali P17137.
    SMRi P17137. Positions 60-259.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH11. Glycoside Hydrolase Family 11.

    Proteomic databases

    PRIDEi P17137.

    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.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR001137. Glyco_hydro_11.
    IPR013319. Glyco_hydro_11/12.
    IPR018208. Glyco_hydro_11_AS.
    [Graphical view ]
    Pfami PF00457. Glyco_hydro_11. 1 hit.
    [Graphical view ]
    PRINTSi PR00911. GLHYDRLASE11.
    SUPFAMi SSF49899. SSF49899. 1 hit.
    PROSITEi PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
    PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of a Clostridium acetobutylicum P262 xylanase gene (xynB)."
      Zappe H., Jones W.A., Woods D.R.
      Nucleic Acids Res. 18:2179-2179(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC BAA-117 / DSM 13864 / NCP 262.

    Entry informationi

    Entry nameiXYNA_CLOSA
    AccessioniPrimary (citable) accession number: P17137
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: August 1, 1990
    Last modified: October 1, 2014
    This is version 79 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Caution

    Was originally thought to originate from C.acetobutylicum.1 Publication

    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