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)

P10478

- XYNZ_CLOTH

UniProt

P10478 - XYNZ_CLOTH

Protein

Endo-1,4-beta-xylanase Z

Gene

xynZ

Organism
Clostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium thermocellum)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 3 (01 Nov 1991)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei645 – 6451Proton donor
    Active sitei754 – 7541Nucleophile

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. endo-1,4-beta-xylanase activity Source: MENGO
    3. xylan endo-1,3-beta-xylosidase activity Source: MENGO

    GO - Biological processi

    1. xylan catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

    Enzyme and pathway databases

    BioCyciCTHE203119:GIW8-2026-MONOMER.
    MetaCyc:MONOMER-16453.
    BRENDAi3.1.1.73. 1530.

    Protein family/group databases

    CAZyiCBM6. Carbohydrate-Binding Module Family 6.
    GH10. Glycoside Hydrolase Family 10.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Endo-1,4-beta-xylanase Z (EC:3.2.1.8)
    Short name:
    Xylanase Z
    Alternative name(s):
    1,4-beta-D-xylan xylanohydrolase Z
    Gene namesi
    Name:xynZ
    Ordered Locus Names:Cthe_1963
    OrganismiClostridium thermocellum (strain ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Ruminiclostridium thermocellum)
    Taxonomic identifieri203119 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium
    ProteomesiUP000002145: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2828Sequence AnalysisAdd
    BLAST
    Chaini29 – 837809Endo-1,4-beta-xylanase ZPRO_0000007973Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi783 ↔ 789By similarity

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Protein-protein interaction databases

    IntActiP10478. 1 interaction.
    STRINGi203119.Cthe_1963.

    Structurei

    Secondary structure

    1
    837
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni37 – 404
    Beta strandi50 – 589
    Turni59 – 624
    Beta strandi63 – 719
    Beta strandi83 – 875
    Turni94 – 1029
    Helixi104 – 11310
    Beta strandi121 – 1255
    Helixi137 – 14711
    Helixi149 – 1568
    Helixi163 – 1653
    Beta strandi166 – 1716
    Helixi173 – 18311
    Turni186 – 1883
    Beta strandi190 – 1967
    Helixi204 – 2074
    Turni209 – 2124
    Helixi213 – 2186
    Beta strandi220 – 2278
    Helixi233 – 24513
    Beta strandi251 – 2555
    Helixi262 – 27918
    Turni280 – 2823
    Helixi518 – 5247
    Beta strandi528 – 5336
    Helixi536 – 5394
    Helixi543 – 55210
    Beta strandi554 – 5607
    Helixi564 – 5674
    Helixi577 – 58812
    Beta strandi592 – 5998
    Beta strandi601 – 6033
    Helixi606 – 6094
    Helixi615 – 63218
    Turni633 – 6364
    Beta strandi638 – 6458
    Beta strandi651 – 6544
    Helixi658 – 6636
    Helixi667 – 67812
    Beta strandi682 – 6909
    Beta strandi692 – 6954
    Helixi696 – 71015
    Beta strandi717 – 7204
    Beta strandi723 – 7275
    Helixi730 – 74516
    Beta strandi749 – 76012
    Helixi765 – 78521
    Beta strandi789 – 7957
    Helixi804 – 8074
    Beta strandi815 – 8173
    Helixi825 – 83410

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1JJFX-ray1.75A20-287[»]
    1JT2X-ray1.80A20-287[»]
    1XYZX-ray1.40A/B491-837[»]
    ProteinModelPortaliP10478.
    SMRiP10478. Positions 30-284, 299-419, 516-835.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP10478.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini299 – 420122CBM6PROSITE-ProRule annotationAdd
    BLAST
    Repeati430 – 453241Add
    BLAST
    Repeati464 – 487242Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni430 – 487582 X 24 AA approximate repeatsAdd
    BLAST

    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

    Contains 1 CBM6 (carbohydrate binding type-6) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG3693.
    KOiK01181.
    OMAiFRYAREA.
    OrthoDBiEOG6XQ3JG.

    Family and domain databases

    Gene3Di1.10.1330.10. 1 hit.
    2.60.120.260. 1 hit.
    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.
    IPR006584. Cellulose-bd_IV.
    IPR005084. CMB_fam6.
    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]
    PfamiPF03422. CBM_6. 1 hit.
    PF00404. Dockerin_1. 2 hits.
    PF00756. Esterase. 1 hit.
    PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view]
    PRINTSiPR00134. GLHYDRLASE10.
    SMARTiSM00606. CBD_IV. 1 hit.
    SM00633. Glyco_10. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    SSF53474. SSF53474. 1 hit.
    SSF63446. SSF63446. 1 hit.
    PROSITEiPS51175. CBM6. 1 hit.
    PS00448. 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.

    P10478-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSRKLFSVLL VGLMLMTSLL VTISSTSAAS LPTMPPSGYD QVRNGVPRGQ    50
    VVNISYFSTA TNSTRPARVY LPPGYSKDKK YSVLYLLHGI GGSENDWFEG 100
    GGRANVIADN LIAEGKIKPL IIVTPNTNAA GPGIADGYEN FTKDLLNSLI 150
    PYIESNYSVY TDREHRAIAG LSMGGGQSFN IGLTNLDKFA YIGPISAAPN 200
    TYPNERLFPD GGKAAREKLK LLFIACGTND SLIGFGQRVH EYCVANNINH 250
    VYWLIQGGGH DFNVWKPGLW NFLQMADEAG LTRDGNTPVP TPSPKPANTR 300
    IEAEDYDGIN SSSIEIIGVP PEGGRGIGYI TSGDYLVYKS IDFGNGATSF 350
    KAKVANANTS NIELRLNGPN GTLIGTLSVK STGDWNTYEE QTCSISKVTG 400
    INDLYLVFKG PVNIDWFTFG VESSSTGLGD LNGDGNINSS DLQALKRHLL 450
    GISPLTGEAL LRADVNRSGK VDSTDYSVLK RYILRIITEF PGQGDVQTPN 500
    PSVTPTQTPI PTISGNALRD YAEARGIKIG TCVNYPFYNN SDPTYNSILQ 550
    REFSMVVCEN EMKFDALQPR QNVFDFSKGD QLLAFAERNG MQMRGHTLIW 600
    HNQNPSWLTN GNWNRDSLLA VMKNHITTVM THYKGKIVEW DVANECMDDS 650
    GNGLRSSIWR NVIGQDYLDY AFRYAREADP DALLFYNDYN IEDLGPKSNA 700
    VFNMIKSMKE RGVPIDGVGF QCHFINGMSP EYLASIDQNI KRYAEIGVIV 750
    SFTEIDIRIP QSENPATAFQ VQANNYKELM KICLANPNCN TFVMWGFTDK 800
    YTWIPGTFPG YGNPLIYDSN YNPKPAYNAI KEALMGY 837
    Length:837
    Mass (Da):92,263
    Last modified:November 1, 1991 - v3
    Checksum:iDD4C29F04D12B6CD
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22624 Genomic DNA. Translation: AAA23286.1.
    CP000568 Genomic DNA. Translation: ABN53181.1.
    PIRiA31842.
    RefSeqiWP_003513959.1. NC_009012.1.
    YP_001038374.1. NC_009012.1.

    Genome annotation databases

    EnsemblBacteriaiABN53181; ABN53181; Cthe_1963.
    GeneIDi4810746.
    KEGGicth:Cthe_1963.
    PATRICi19517811. VBICloThe47081_2079.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22624 Genomic DNA. Translation: AAA23286.1 .
    CP000568 Genomic DNA. Translation: ABN53181.1 .
    PIRi A31842.
    RefSeqi WP_003513959.1. NC_009012.1.
    YP_001038374.1. NC_009012.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1JJF X-ray 1.75 A 20-287 [» ]
    1JT2 X-ray 1.80 A 20-287 [» ]
    1XYZ X-ray 1.40 A/B 491-837 [» ]
    ProteinModelPortali P10478.
    SMRi P10478. Positions 30-284, 299-419, 516-835.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P10478. 1 interaction.
    STRINGi 203119.Cthe_1963.

    Protein family/group databases

    CAZyi CBM6. Carbohydrate-Binding Module Family 6.
    GH10. Glycoside Hydrolase Family 10.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABN53181 ; ABN53181 ; Cthe_1963 .
    GeneIDi 4810746.
    KEGGi cth:Cthe_1963.
    PATRICi 19517811. VBICloThe47081_2079.

    Phylogenomic databases

    eggNOGi COG3693.
    KOi K01181.
    OMAi FRYAREA.
    OrthoDBi EOG6XQ3JG.

    Enzyme and pathway databases

    BioCyci CTHE203119:GIW8-2026-MONOMER.
    MetaCyc:MONOMER-16453.
    BRENDAi 3.1.1.73. 1530.

    Miscellaneous databases

    EvolutionaryTracei P10478.

    Family and domain databases

    Gene3Di 1.10.1330.10. 1 hit.
    2.60.120.260. 1 hit.
    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.
    IPR006584. Cellulose-bd_IV.
    IPR005084. CMB_fam6.
    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 PF03422. CBM_6. 1 hit.
    PF00404. Dockerin_1. 2 hits.
    PF00756. Esterase. 1 hit.
    PF00331. Glyco_hydro_10. 1 hit.
    [Graphical view ]
    PRINTSi PR00134. GLHYDRLASE10.
    SMARTi SM00606. CBD_IV. 1 hit.
    SM00633. Glyco_10. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49785. SSF49785. 1 hit.
    SSF51445. SSF51445. 1 hit.
    SSF53474. SSF53474. 1 hit.
    SSF63446. SSF63446. 1 hit.
    PROSITEi PS51175. CBM6. 1 hit.
    PS00448. CLOS_CELLULOSOME_RPT. 2 hits.
    PS00018. EF_HAND_1. 2 hits.
    PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence and deletion analysis of the xylanase gene (xynZ) of Clostridium thermocellum."
      Grepinet O., Chebrou M.-C., Beguin P.
      J. Bacteriol. 170:4582-4588(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 27405 / DSM 1237 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372.
    3. "A common protein fold and similar active site in two distinct families of beta-glycanases."
      Dominguez R., Souchon H., Spinelli S., Dauter Z., Wilson K.S., Chauvaux S., Beguin P., Alzari P.M.
      Nat. Struct. Biol. 2:569-576(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 515-837.

    Entry informationi

    Entry nameiXYNZ_CLOTH
    AccessioniPrimary (citable) accession number: P10478
    Secondary accession number(s): A3DGV2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: November 1, 1991
    Last modified: October 1, 2014
    This is version 120 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    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