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P54865

- XYND_CELFI

UniProt

P54865 - XYND_CELFI

Protein

Bifunctional xylanase/deacetylase

Gene

xynD

Organism
Cellulomonas fimi
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Endo-acting xylanase which displays no detectable activity against polysaccharides other than xylan. Hydrolyzes glucosidic bonds with retention of anomeric configuration.

    Catalytic activityi

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

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei126 – 1261NucleophilePROSITE-ProRule annotation
    Active sitei216 – 2161Proton donorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC
    2. hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds Source: InterPro
    3. polysaccharide binding Source: InterPro

    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

    BRENDAi3.2.1.8. 1233.
    UniPathwayiUPA00114.

    Protein family/group databases

    CAZyiCBM2. Carbohydrate-Binding Module Family 2.
    GH11. Glycoside Hydrolase Family 11.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional xylanase/deacetylase
    Including the following 2 domains:
    Endo-1,4-beta-xylanase D (EC:3.2.1.8)
    Short name:
    XYLD
    Short name:
    Xylanase D
    Acetylated xylan deacetylase (EC:3.5.1.-)
    Gene namesi
    Name:xynD
    OrganismiCellulomonas fimi
    Taxonomic identifieri1708 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4343Sequence AnalysisAdd
    BLAST
    Chaini44 – 644601Bifunctional xylanase/deacetylasePRO_0000008000Add
    BLAST

    Structurei

    Secondary structure

    1
    644
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi250 – 2523
    Beta strandi255 – 2584
    Beta strandi260 – 2689
    Beta strandi278 – 2803
    Beta strandi287 – 2937
    Beta strandi296 – 3005
    Beta strandi302 – 3043
    Beta strandi311 – 3188
    Beta strandi327 – 3293
    Beta strandi562 – 5654
    Beta strandi571 – 5799
    Beta strandi589 – 5913
    Beta strandi601 – 6077
    Beta strandi609 – 6168
    Beta strandi618 – 6203
    Beta strandi622 – 6298

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1E5BNMR-A247-333[»]
    1E5CNMR-A247-333[»]
    1HEHNMR-C557-644[»]
    1HEJNMR-C557-644[»]
    1XBDNMR-A247-333[»]
    2XBDNMR-A247-333[»]
    ProteinModelPortaliP54865.
    SMRiP54865. Positions 15-235, 247-333, 356-544, 557-644.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP54865.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini246 – 33388CBM2 1Add
    BLAST
    Domaini356 – 532177NodB homologyPROSITE-ProRule annotationAdd
    BLAST
    Domaini557 – 64488CBM2 2Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni44 – 230187EndoglucanaseAdd
    BLAST
    Regioni231 – 24515Linker ("hinge") (Gly-rich box)Add
    BLAST
    Regioni337 – 35014Linker ("hinge") (Pro-Thr box)Add
    BLAST
    Regioni548 – 5569Linker ("hinge") (Gly-rich box)

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi231 – 2388Poly-Gly

    Sequence similaritiesi

    Contains 1 NodB homology domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di2.60.120.180. 1 hit.
    2.60.40.290. 2 hits.
    3.20.20.370. 1 hit.
    InterProiIPR008965. Carb-bd_dom.
    IPR012291. CBD_carb-bd_dom.
    IPR001919. Cellulose-bd_dom_fam2_bac.
    IPR008985. ConA-like_lec_gl_sf.
    IPR011330. Glyco_hydro/deAcase_b/a-brl.
    IPR001137. Glyco_hydro_11.
    IPR013319. Glyco_hydro_11/12.
    IPR018208. Glyco_hydro_11_AS.
    IPR002509. Polysac_deacetylase.
    IPR006311. TAT_signal.
    [Graphical view]
    PfamiPF00553. CBM_2. 2 hits.
    PF00457. Glyco_hydro_11. 1 hit.
    PF01522. Polysacc_deac_1. 1 hit.
    [Graphical view]
    PRINTSiPR00911. GLHYDRLASE11.
    SMARTiSM00637. CBD_II. 2 hits.
    [Graphical view]
    SUPFAMiSSF49384. SSF49384. 2 hits.
    SSF49899. SSF49899. 1 hit.
    SSF88713. SSF88713. 1 hit.
    PROSITEiPS51173. CBM2. 2 hits.
    PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
    PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
    PS51677. NODB. 1 hit.
    PS51318. TAT. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P54865-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDSFEATRT TRRRRPLQAL TGLLAAGALV AGALAAASPA AAAVTSNTTG    50
    THDGYFYSFW TDSPGSVSMD LNSGGGYTRW SNTGNFVAGK GWSTGGRKTV 100
    SYSGQFNPSR NAYLTLYGWT QSPLVEYYIV DSWGTYRPTG TFMGTVTSDG 150
    GTYDIYRTQR VNKPSIEGDS STFYQYWSVR QQKRTGGTIT SGNHFDAWAS 200
    KGMNLGRHNY MIMATEGYQS SGSSSITVSE GSGGGGGGDT GGGGGSTGCS 250
    VTATRAEEWS DRFNVTYSVS GSSAWTVNLA LNGSQTIQAS WNANVTGSGS 300
    TRTVTPNGSG NTFGVTVMKN GSSTTPAATC AGSGGGTATP TPTPTPTPTP 350
    QSCSAGYVGL TFDDGPNTGT TNQILSTLTQ YGATATVFPT GQNAQGNPSL 400
    MQAYKNAGVQ IGNHSWDHPH LVNMSQSDMQ SQLTRTQQAI QQTAGVTPTL 450
    FRPPYGESNA TLRQVESSLG LREIIWDVDS QDWNNASASQ IRQAASRLTN 500
    GQIILMHDWP AATVQALPGI LQDLRSRNLC TGHISSSTGR AVAPSSAGGG 550
    GGGGGGTGSC SVSAVRGEEW ADRFNVTYSV SGSSSWVVTL GLNGGQSVQS 600
    SWNAALTGSS GTVTARPNGS GNSFGVTFYK NGSSATPGAT CATG 644
    Length:644
    Mass (Da):66,582
    Last modified:October 1, 1996 - v1
    Checksum:i56B045CC6E0E1820
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76729 Genomic DNA. Translation: CAA54145.1.
    PIRiI40712.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76729 Genomic DNA. Translation: CAA54145.1 .
    PIRi I40712.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1E5B NMR - A 247-333 [» ]
    1E5C NMR - A 247-333 [» ]
    1HEH NMR - C 557-644 [» ]
    1HEJ NMR - C 557-644 [» ]
    1XBD NMR - A 247-333 [» ]
    2XBD NMR - A 247-333 [» ]
    ProteinModelPortali P54865.
    SMRi P54865. Positions 15-235, 247-333, 356-544, 557-644.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi CBM2. Carbohydrate-Binding Module Family 2.
    GH11. Glycoside Hydrolase Family 11.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00114 .
    BRENDAi 3.2.1.8. 1233.

    Miscellaneous databases

    EvolutionaryTracei P54865.

    Family and domain databases

    Gene3Di 2.60.120.180. 1 hit.
    2.60.40.290. 2 hits.
    3.20.20.370. 1 hit.
    InterProi IPR008965. Carb-bd_dom.
    IPR012291. CBD_carb-bd_dom.
    IPR001919. Cellulose-bd_dom_fam2_bac.
    IPR008985. ConA-like_lec_gl_sf.
    IPR011330. Glyco_hydro/deAcase_b/a-brl.
    IPR001137. Glyco_hydro_11.
    IPR013319. Glyco_hydro_11/12.
    IPR018208. Glyco_hydro_11_AS.
    IPR002509. Polysac_deacetylase.
    IPR006311. TAT_signal.
    [Graphical view ]
    Pfami PF00553. CBM_2. 2 hits.
    PF00457. Glyco_hydro_11. 1 hit.
    PF01522. Polysacc_deac_1. 1 hit.
    [Graphical view ]
    PRINTSi PR00911. GLHYDRLASE11.
    SMARTi SM00637. CBD_II. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49384. SSF49384. 2 hits.
    SSF49899. SSF49899. 1 hit.
    SSF88713. SSF88713. 1 hit.
    PROSITEi PS51173. CBM2. 2 hits.
    PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
    PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
    PS51677. NODB. 1 hit.
    PS51318. TAT. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Evidence for a general role for high-affinity non-catalytic cellulose binding domains in microbial plant cell wall hydrolases."
      Millward-Sadler S.J., Poole D.M., Henrissat B., Hazlewood G.P., Clarke J.H., Gilbert H.J.
      Mol. Microbiol. 11:375-382(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 221.

    Entry informationi

    Entry nameiXYND_CELFI
    AccessioniPrimary (citable) accession number: P54865
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 97 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Multifunctional enzyme

    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