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)

P51584

- XYNY_CLOTM

UniProt

P51584 - XYNY_CLOTM

Protein

Endo-1,4-beta-xylanase Y

Gene

xynY

Organism
Clostridium thermocellum (Ruminiclostridium thermocellum)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

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

    pH dependencei

    Optimum pH is 6.8.

    Temperature dependencei

    Optimum temperature is 75 degrees Celsius.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei337 – 3371Proton donorBy similarity
    Active sitei460 – 4601NucleophilePROSITE-ProRule annotation

    GO - Molecular functioni

    1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC

    GO - Biological processi

    1. xylan catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Protein family/group databases

    CAZyiCBM22. Carbohydrate-Binding Module Family 22.
    GH10. Glycoside Hydrolase Family 10.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-1,4-beta-xylanase Y (EC:3.2.1.8)
    Short name:
    Xylanase Y
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase Y
    Short name:
    XylY
    Gene namesi
    Name:xynY
    OrganismiClostridium thermocellum (Ruminiclostridium thermocellum)
    Taxonomic identifieri1515 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

    Subcellular locationi

    GO - Cellular componenti

    1. cellulosome Source: MENGO

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Sequence AnalysisAdd
    BLAST
    Chaini27 – 10771051Endo-1,4-beta-xylanase YPRO_0000007972Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    DIPiDIP-35413N.
    IntActiP51584. 1 interaction.

    Structurei

    Secondary structure

    1
    1077
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 396
    Beta strandi42 – 443
    Beta strandi48 – 525
    Beta strandi56 – 605
    Helixi65 – 673
    Beta strandi70 – 745
    Beta strandi78 – 803
    Beta strandi82 – 865
    Turni88 – 903
    Beta strandi96 – 1049
    Beta strandi107 – 12115
    Turni122 – 1243
    Beta strandi127 – 13812
    Beta strandi143 – 1508
    Beta strandi155 – 16612
    Beta strandi170 – 17910
    Helixi195 – 1984
    Turni199 – 2024
    Beta strandi204 – 2096
    Helixi213 – 2153
    Helixi217 – 22610
    Beta strandi228 – 2347
    Helixi238 – 2414
    Beta strandi242 – 2487
    Beta strandi251 – 2544
    Turni257 – 2593
    Helixi260 – 2689
    Beta strandi272 – 2798
    Beta strandi281 – 2833
    Helixi286 – 2894
    Beta strandi293 – 2975
    Helixi302 – 32322
    Beta strandi329 – 3379
    Helixi343 – 3486
    Beta strandi355 – 3584
    Helixi363 – 3686
    Helixi373 – 38412
    Beta strandi390 – 3978
    Helixi401 – 41616
    Beta strandi422 – 4254
    Beta strandi428 – 4314
    Beta strandi433 – 4353
    Helixi439 – 45012
    Beta strandi453 – 46412
    Turni466 – 4694
    Helixi472 – 49221
    Beta strandi498 – 50710
    Helixi515 – 5173
    Beta strandi520 – 5223
    Helixi530 – 5356
    Helixi541 – 5433
    Beta strandi566 – 5716
    Beta strandi581 – 5833
    Beta strandi587 – 5937
    Beta strandi596 – 5994
    Beta strandi601 – 6055
    Beta strandi613 – 6186
    Turni620 – 6223
    Beta strandi628 – 6369
    Beta strandi639 – 6424
    Beta strandi644 – 65310
    Beta strandi659 – 66911
    Beta strandi675 – 6839
    Beta strandi689 – 69911
    Beta strandi704 – 71310
    Beta strandi738 – 7403
    Helixi743 – 75311
    Helixi761 – 7677
    Helixi777 – 78711
    Helixi817 – 8204
    Beta strandi828 – 8369
    Beta strandi839 – 8479
    Beta strandi858 – 8636
    Turni876 – 8783
    Helixi880 – 88910
    Beta strandi896 – 9005
    Turni910 – 9123
    Helixi913 – 9197
    Helixi921 – 9288
    Beta strandi934 – 9374
    Helixi938 – 9425
    Helixi943 – 9475
    Beta strandi948 – 9536
    Helixi955 – 96713
    Turni968 – 9703
    Beta strandi973 – 9786
    Beta strandi983 – 9864
    Helixi987 – 100115
    Beta strandi1009 – 10157
    Helixi1021 – 103212
    Beta strandi1039 – 10413
    Turni1043 – 10453
    Beta strandi1048 – 10536
    Helixi1060 – 107011
    Helixi1071 – 10733

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1DYOX-ray2.10A/B558-718[»]
    1GKKX-ray1.60A/B792-1077[»]
    1GKLX-ray1.40A/B792-1077[»]
    1H6XX-ray2.23A560-720[»]
    1H6YX-ray2.12A/B560-720[»]
    1OHZX-ray2.20B733-791[»]
    1WB4X-ray1.40A/B792-1077[»]
    1WB5X-ray1.40A/B792-1077[»]
    1WB6X-ray1.40A/B792-1077[»]
    2CCLX-ray2.03B/D730-791[»]
    2W5FX-ray1.90A/B32-551[»]
    2WYSX-ray2.75A/B33-551[»]
    2WZEX-ray2.50A/B33-551[»]
    3ZI7X-ray2.30A/B792-1077[»]
    4BAGX-ray1.90A/B792-1077[»]
    4H35X-ray1.90A/B792-1077[»]
    ProteinModelPortaliP51584.
    SMRiP51584. Positions 561-719, 733-788, 803-1075.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51584.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 180148CBM-cenC 1Add
    BLAST
    Domaini565 – 714150CBM-cenC 2Add
    BLAST
    Repeati734 – 757241Add
    BLAST
    Repeati768 – 791242Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni255 – 512258CatalyticSequence AnalysisAdd
    BLAST
    Regioni734 – 791582 X 24 AA approximate repeatsAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi552 – 5576Poly-Gly

    Domaini

    A 24 residue domain is repeated twice in this enzyme as well as in other C.thermocellum cellulosome enzymes. This domain may function as the binding ligand for the SL component.

    Sequence similaritiesi

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di1.10.1330.10. 1 hit.
    2.60.120.260. 2 hits.
    3.20.20.80. 1 hit.
    3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR016134. Cellulos_enz_dockerin_1.
    IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
    IPR003305. CenC_carb-bd.
    IPR018242. Dockerin_1.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR000801. Esterase_put.
    IPR008979. Galactose-bd-like.
    IPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view]
    PfamiPF02018. CBM_4_9. 2 hits.
    PF00404. Dockerin_1. 2 hits.
    PF00756. Esterase. 1 hit.
    PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view]
    PRINTSiPR00134. GLHYDRLASE10.
    SMARTiSM00633. Glyco_10. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 2 hits.
    SSF51445. SSF51445. 1 hit.
    SSF53474. SSF53474. 1 hit.
    SSF63446. SSF63446. 1 hit.
    PROSITEiPS00448. CLOS_CELLULOSOME_RPT. 2 hits.
    PS00018. EF_HAND_1. 2 hits.
    PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P51584-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKNKRVLAKI TALVVLLGVF FVLPSNISQL YADYEVVHDT FEVNFDGWCN     50
    LGVDTYLTAV ENEGNNGTRG MMVINRSSAS DGAYSEKGFY LDGGVEYKYS 100
    VFVKHNGTGT ETFKLSVSYL DSETEEENKE VIATKDVVAG EWTEISAKYK 150
    APKTAVNITL SITTDSTVDF IFDDVTITRK GMAEANTVYA ANAVLKDMYA 200
    NYFRVGSVLN SGTVNNSSIK ALILREFNSI TCENEMKPDA TLVQSGSTNT 250
    NIRVSLNRAA SILNFCAQNN IAVRGHTLVW HSQTPQWFFK DNFQDNGNWV 300
    SQSVMDQRLE SYIKNMFAEI QRQYPSLNLY AYDVVNEAVS DDANRTRYYG 350
    GAREPGYGNG RSPWVQIYGD NKFIEKAFTY ARKYAPANCK LYYNDYNEYW 400
    DHKRDCIASI CANLYNKGLL DGVGMQSHIN ADMNGFSGIQ NYKAALQKYI 450
    NIGCDVQITE LDISTENGKF SLQQQADKYK AVFQAAVDIN RTSSKGKVTA 500
    VCVWGPNDAN TWLGSQNAPL LFNANNQPKP AYNAVASIIP QSEWGDGNNP 550
    AGGGGGGKPE EPDANGYYYH DTFEGSVGQW TARGPAEVLL SGRTAYKGSE 600
    SLLVRNRTAA WNGAQRALNP RTFVPGNTYC FSVVASFIEG ASSTTFCMKL 650
    QYVDGSGTQR YDTIDMKTVG PNQWVHLYNP QYRIPSDATD MYVYVETADD 700
    TINFYIDEAI GAVAGTVIEG PAPQPTQPPV LLGDVNGDGT INSTDLTMLK 750
    RSVLRAITLT DDAKARADVD KNGSINSTDV LLLSRYLLRV IDKFPVAENP 800
    SSSFKYESAV QYRPAPDSYL NPCPQAGRIV KETYTGINGT KSLNVYLPYG 850
    YDPNKKYNIF YLMHGGGENE NTIFSNDVKL QNILDHAIMN GELEPLIVVT 900
    PTFNGGNCTA QNFYQEFRQN VIPFVESKYS TYAESTTPQG IAASRMHRGF 950
    GGFSMGGLTT WYVMVNCLDY VAYFMPLSGD YWYGNSPQDK ANSIAEAINR 1000
    SGLSKREYFV FAATGSDHIA YANMNPQIEA MKALPHFDYT SDFSKGNFYF 1050
    LVAPGATHWW GYVRHYIYDA LPYFFHE 1077
    Length:1,077
    Mass (Da):119,673
    Last modified:October 1, 1996 - v1
    Checksum:iBFC8D2D22C5726A0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83269 Genomic DNA. Translation: CAA58242.1.
    PIRiS54975.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X83269 Genomic DNA. Translation: CAA58242.1 .
    PIRi S54975.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1DYO X-ray 2.10 A/B 558-718 [» ]
    1GKK X-ray 1.60 A/B 792-1077 [» ]
    1GKL X-ray 1.40 A/B 792-1077 [» ]
    1H6X X-ray 2.23 A 560-720 [» ]
    1H6Y X-ray 2.12 A/B 560-720 [» ]
    1OHZ X-ray 2.20 B 733-791 [» ]
    1WB4 X-ray 1.40 A/B 792-1077 [» ]
    1WB5 X-ray 1.40 A/B 792-1077 [» ]
    1WB6 X-ray 1.40 A/B 792-1077 [» ]
    2CCL X-ray 2.03 B/D 730-791 [» ]
    2W5F X-ray 1.90 A/B 32-551 [» ]
    2WYS X-ray 2.75 A/B 33-551 [» ]
    2WZE X-ray 2.50 A/B 33-551 [» ]
    3ZI7 X-ray 2.30 A/B 792-1077 [» ]
    4BAG X-ray 1.90 A/B 792-1077 [» ]
    4H35 X-ray 1.90 A/B 792-1077 [» ]
    ProteinModelPortali P51584.
    SMRi P51584. Positions 561-719, 733-788, 803-1075.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35413N.
    IntActi P51584. 1 interaction.

    Protein family/group databases

    CAZyi CBM22. Carbohydrate-Binding Module Family 22.
    GH10. Glycoside Hydrolase Family 10.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P51584.

    Family and domain databases

    Gene3Di 1.10.1330.10. 1 hit.
    2.60.120.260. 2 hits.
    3.20.20.80. 1 hit.
    3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR016134. Cellulos_enz_dockerin_1.
    IPR002105. Cellulos_enz_dockerin_1_Ca-bd.
    IPR003305. CenC_carb-bd.
    IPR018242. Dockerin_1.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR000801. Esterase_put.
    IPR008979. Galactose-bd-like.
    IPR001000. Glyco_hydro_10.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF02018. CBM_4_9. 2 hits.
    PF00404. Dockerin_1. 2 hits.
    PF00756. Esterase. 1 hit.
    PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view ]
    PRINTSi PR00134. GLHYDRLASE10.
    SMARTi SM00633. Glyco_10. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49785. SSF49785. 2 hits.
    SSF51445. SSF51445. 1 hit.
    SSF53474. SSF53474. 1 hit.
    SSF63446. SSF63446. 1 hit.
    PROSITEi PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
    PS00018. EF_HAND_1. 2 hits.
    PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Evidence for a general role for non-catalytic thermostabilizing domains in xylanases from thermophilic bacteria."
      Fontes C.M.G.A., Hazelwood G.P., Morag E., Hall J., Hirst B.H., Gilbert H.J.
      Biochem. J. 307:151-158(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: YS.

    Entry informationi

    Entry nameiXYNY_CLOTM
    AccessioniPrimary (citable) accession number: P51584
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 104 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

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3