Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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: Annotation score: 3 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)DescriptionActionsGraphical viewLength
Active sitei645Proton donor1
Active sitei754Nucleophile1

GO - Molecular functioni

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16453.
BRENDAi3.1.1.73. 1530.
3.2.1.8. 1530.

Protein family/group databases

CAZyiCBM6. Carbohydrate-Binding Module Family 6.
GH10. Glycoside Hydrolase Family 10.
ESTHERiclotm-xynz. A85-Feruloyl-Esterase.

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
Proteomesi
  • UP000002145 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 28Sequence analysisAdd BLAST28
ChainiPRO_000000797329 – 837Endo-1,4-beta-xylanase ZAdd BLAST809

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi783 ↔ 789By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

IntActiP10478. 1 interactor.
STRINGi203119.Cthe_1963.

Structurei

Secondary structure

1837
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni37 – 40Combined sources4
Beta strandi50 – 58Combined sources9
Turni59 – 62Combined sources4
Beta strandi63 – 71Combined sources9
Beta strandi83 – 87Combined sources5
Turni94 – 102Combined sources9
Helixi104 – 113Combined sources10
Beta strandi121 – 125Combined sources5
Helixi137 – 147Combined sources11
Helixi149 – 156Combined sources8
Helixi163 – 165Combined sources3
Beta strandi166 – 171Combined sources6
Helixi173 – 183Combined sources11
Turni186 – 188Combined sources3
Beta strandi190 – 196Combined sources7
Helixi204 – 207Combined sources4
Turni209 – 212Combined sources4
Helixi213 – 218Combined sources6
Beta strandi220 – 227Combined sources8
Helixi233 – 245Combined sources13
Beta strandi251 – 255Combined sources5
Helixi262 – 279Combined sources18
Turni280 – 282Combined sources3
Helixi518 – 524Combined sources7
Beta strandi528 – 533Combined sources6
Helixi536 – 539Combined sources4
Helixi543 – 552Combined sources10
Beta strandi554 – 560Combined sources7
Helixi564 – 567Combined sources4
Helixi577 – 588Combined sources12
Beta strandi592 – 599Combined sources8
Beta strandi601 – 603Combined sources3
Helixi606 – 609Combined sources4
Helixi615 – 632Combined sources18
Turni633 – 636Combined sources4
Beta strandi638 – 645Combined sources8
Beta strandi651 – 654Combined sources4
Helixi658 – 663Combined sources6
Helixi667 – 678Combined sources12
Beta strandi682 – 690Combined sources9
Beta strandi692 – 695Combined sources4
Helixi696 – 710Combined sources15
Beta strandi717 – 720Combined sources4
Beta strandi723 – 727Combined sources5
Helixi730 – 745Combined sources16
Beta strandi749 – 760Combined sources12
Helixi765 – 785Combined sources21
Beta strandi789 – 795Combined sources7
Helixi804 – 807Combined sources4
Beta strandi815 – 817Combined sources3
Helixi825 – 834Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JJFX-ray1.75A20-287[»]
1JT2X-ray1.80A20-287[»]
1XYZX-ray1.40A/B491-837[»]
ProteinModelPortaliP10478.
SMRiP10478.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP10478.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini299 – 420CBM6PROSITE-ProRule annotationAdd BLAST122
Domaini424 – 492DockerinPROSITE-ProRule annotationAdd BLAST69
Domaini512 – 833GH10PROSITE-ProRule annotationAdd BLAST322

Sequence similaritiesi

Contains 1 CBM6 (carbohydrate binding type-6) domain.PROSITE-ProRule annotation
Contains 1 dockerin domain.PROSITE-ProRule annotation
Contains 1 GH10 (glycosyl hydrolase family 10) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG2382. LUCA.
COG3693. LUCA.
KOiK01181.
OMAiEMKFDAL.
OrthoDBiPOG091H0560.

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.
IPR006584. Cellulose-bd_IV.
IPR005084. CMB_fam6.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR000801. Esterase_put.
IPR008979. Galactose-bd-like.
IPR001000. GH10.
IPR031158. GH10_AS.
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.
PS51766. DOCKERIN. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS00591. GH10_1. 1 hit.
PS51760. GH10_2. 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

        10         20         30         40         50
MSRKLFSVLL VGLMLMTSLL VTISSTSAAS LPTMPPSGYD QVRNGVPRGQ
60 70 80 90 100
VVNISYFSTA TNSTRPARVY LPPGYSKDKK YSVLYLLHGI GGSENDWFEG
110 120 130 140 150
GGRANVIADN LIAEGKIKPL IIVTPNTNAA GPGIADGYEN FTKDLLNSLI
160 170 180 190 200
PYIESNYSVY TDREHRAIAG LSMGGGQSFN IGLTNLDKFA YIGPISAAPN
210 220 230 240 250
TYPNERLFPD GGKAAREKLK LLFIACGTND SLIGFGQRVH EYCVANNINH
260 270 280 290 300
VYWLIQGGGH DFNVWKPGLW NFLQMADEAG LTRDGNTPVP TPSPKPANTR
310 320 330 340 350
IEAEDYDGIN SSSIEIIGVP PEGGRGIGYI TSGDYLVYKS IDFGNGATSF
360 370 380 390 400
KAKVANANTS NIELRLNGPN GTLIGTLSVK STGDWNTYEE QTCSISKVTG
410 420 430 440 450
INDLYLVFKG PVNIDWFTFG VESSSTGLGD LNGDGNINSS DLQALKRHLL
460 470 480 490 500
GISPLTGEAL LRADVNRSGK VDSTDYSVLK RYILRIITEF PGQGDVQTPN
510 520 530 540 550
PSVTPTQTPI PTISGNALRD YAEARGIKIG TCVNYPFYNN SDPTYNSILQ
560 570 580 590 600
REFSMVVCEN EMKFDALQPR QNVFDFSKGD QLLAFAERNG MQMRGHTLIW
610 620 630 640 650
HNQNPSWLTN GNWNRDSLLA VMKNHITTVM THYKGKIVEW DVANECMDDS
660 670 680 690 700
GNGLRSSIWR NVIGQDYLDY AFRYAREADP DALLFYNDYN IEDLGPKSNA
710 720 730 740 750
VFNMIKSMKE RGVPIDGVGF QCHFINGMSP EYLASIDQNI KRYAEIGVIV
760 770 780 790 800
SFTEIDIRIP QSENPATAFQ VQANNYKELM KICLANPNCN TFVMWGFTDK
810 820 830
YTWIPGTFPG YGNPLIYDSN YNPKPAYNAI KEALMGY
Length:837
Mass (Da):92,263
Last modified:November 1, 1991 - v3
Checksum:iDD4C29F04D12B6CD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22624 Genomic DNA. Translation: AAA23286.1.
CP000568 Genomic DNA. Translation: ABN53181.1.
PIRiA31842.
RefSeqiWP_003513959.1. NC_009012.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22624 Genomic DNA. Translation: AAA23286.1.
CP000568 Genomic DNA. Translation: ABN53181.1.
PIRiA31842.
RefSeqiWP_003513959.1. NC_009012.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JJFX-ray1.75A20-287[»]
1JT2X-ray1.80A20-287[»]
1XYZX-ray1.40A/B491-837[»]
ProteinModelPortaliP10478.
SMRiP10478.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP10478. 1 interactor.
STRINGi203119.Cthe_1963.

Protein family/group databases

CAZyiCBM6. Carbohydrate-Binding Module Family 6.
GH10. Glycoside Hydrolase Family 10.
ESTHERiclotm-xynz. A85-Feruloyl-Esterase.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG2382. LUCA.
COG3693. LUCA.
KOiK01181.
OMAiEMKFDAL.
OrthoDBiPOG091H0560.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16453.
BRENDAi3.1.1.73. 1530.
3.2.1.8. 1530.

Miscellaneous databases

EvolutionaryTraceiP10478.

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.
IPR006584. Cellulose-bd_IV.
IPR005084. CMB_fam6.
IPR002105. Dockerin_1_rpt.
IPR016134. Dockerin_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR000801. Esterase_put.
IPR008979. Galactose-bd-like.
IPR001000. GH10.
IPR031158. GH10_AS.
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.
PS51766. DOCKERIN. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS00591. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 132 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.