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P10478

- XYNZ_CLOTH

UniProt

P10478 - XYNZ_CLOTH

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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

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        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.
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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 / 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: November 26, 2014
This is version 121 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