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P10478

- XYNZ_CLOTH

UniProt

P10478 - XYNZ_CLOTH

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Protein

Endo-1,4-beta-xylanase Z

Gene
xynZ, Cthe_1963
Organism
Clostridium thermocellum (strain ATCC 27405 / DSM 1237)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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)
Taxonomic identifieri203119 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium
ProteomesiUP000002145: Chromosome

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Miscellaneous databases

EvolutionaryTraceiP10478.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini299 – 420122CBM6Add
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

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

« Hide 'large scale' publications
  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.
  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: September 3, 2014
This is version 119 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

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

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