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Protein

Endo-1,4-beta-xylanase A

Gene

xynA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
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.

pH dependencei

Optimum pH is 6.2.

Temperature dependencei

Optimum temperature is 90 degrees Celsius. Thermostable.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei502 – 5021Proton donorBy similarity
Active sitei608 – 6081NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. endo-1,4-beta-xylanase activity Source: UniProtKB-EC

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

BioCyciMetaCyc:MONOMER-16897.
BRENDAi3.2.1.8. 6331.

Protein family/group databases

CAZyiCBM22. Carbohydrate-Binding Module Family 22.
CBM9. Carbohydrate-Binding Module Family 9.
GH10. Glycoside Hydrolase Family 10.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase A (EC:3.2.1.8)
Short name:
Xylanase A
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Gene namesi
Name:xynA
Ordered Locus Names:TM_0061
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
ProteomesiUP000008183: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 10591029Endo-1,4-beta-xylanase APRO_0000007986Add
BLAST

Proteomic databases

PRIDEiQ60037.

Interactioni

Protein-protein interaction databases

STRINGi243274.TM0061.

Structurei

Secondary structure

1
1059
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi872 – 8776Combined sources
Beta strandi882 – 8854Combined sources
Helixi888 – 8925Combined sources
Beta strandi895 – 8973Combined sources
Beta strandi900 – 9045Combined sources
Turni906 – 9083Combined sources
Beta strandi911 – 9188Combined sources
Beta strandi920 – 93011Combined sources
Beta strandi938 – 9403Combined sources
Helixi941 – 9433Combined sources
Beta strandi944 – 9529Combined sources
Beta strandi965 – 9717Combined sources
Beta strandi976 – 9783Combined sources
Helixi984 – 9863Combined sources
Beta strandi987 – 9948Combined sources
Beta strandi997 – 10059Combined sources
Beta strandi1015 – 102612Combined sources
Beta strandi1032 – 10398Combined sources
Beta strandi1041 – 10433Combined sources
Turni1045 – 10473Combined sources
Helixi1049 – 10513Combined sources
Beta strandi1052 – 10587Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I82X-ray1.90A871-1059[»]
1I8AX-ray1.90A871-1059[»]
1I8UX-ray1.90A871-1059[»]
ProteinModelPortaliQ60037.
SMRiQ60037. Positions 871-1059.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ60037.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini700 – 870171CBM-cenC 1Add
BLAST
Domaini871 – 1059189CBM-cenC 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni47 – 199153A-1Add
BLAST
Regioni200 – 354155A-2Add
BLAST
Regioni355 – 691337B, catalyticAdd
BLAST

Domaini

The C-terminal CBM-CenC domains mediate the binding of XynA to microcrystalline cellulose. CBM-CenC 2 alone can also promote cellulose binding.

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiCOG3693.
InParanoidiQ60037.
KOiK01181.
OMAiQNPTLEF.
OrthoDBiEOG6B363F.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.1190. 2 hits.
3.20.20.80. 1 hit.
InterProiIPR010502. Carb-bd_dom_fam9.
IPR003305. CenC_carb-bd.
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.
PF06452. DUF1083. 2 hits.
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.
PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q60037-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQVRKRRGLL DVSTAVLVGI LAGFLGVVLA ASGVLSFGKE ASSKGDSSLE
60 70 80 90 100
TVLALSFEGT TEGVVPFGKD VVLTASQDVA ADGEYSLKVE NRTSPWDGVE
110 120 130 140 150
IDLTGKVKSG ADYLLSFQVY QSSDAPQLFN VVARTEDEKG ERYDVILDKV
160 170 180 190 200
VVSDHWKEIL VPFSPTFEGT PAKYSLIIVA SKNTNFNFYL DKVQVLAPKE
210 220 230 240 250
SGPKVIYETS FENGVGDWQP RGDVNIEASS EVAHSGKSSL FISNRQKGWQ
260 270 280 290 300
GAQINLKGIL KTGKTYAFEA WVYQNSGQDQ TIIMTMQRKY SSDASTQYEW
310 320 330 340 350
IKSATVPSGQ WVQLSGTYTI PAGVTVEDLT LYFESQNPTL EFYVDDVKIV
360 370 380 390 400
DTTSAEIKIE MEPEKEIPAL KEVLKDYFKV GVALPSKVFL NPKDIELITK
410 420 430 440 450
HFNSITAENE MKPESLLAGI ENGKLKFRFE TADKYIQFVE ENGMVIRGHT
460 470 480 490 500
LVWHNQTPDW FFKDENGNLL SKEAMTERLK EYIHTVVGHF KGKVYAWDVV
510 520 530 540 550
NEAVDPNQPD GLRRSTWYQI MGPDYIELAF KFAREADPDA KLFYNDYNTF
560 570 580 590 600
EPRKRDIIYN LVKDLKEKGL IDGIGMQCHI SLATDIKQIE EAIKKFSTIP
610 620 630 640 650
GIEIHITELD MSVYRDSSSN YPEAPRTALI EQAHKMMQLF EIFKKYSNVI
660 670 680 690 700
TNVTFWGLKD DYSWRATRRN DWPLIFDKDH QAKLAYWAIV APEVLPPLPK
710 720 730 740 750
ESRISEGEAV VVGMMDDSYL MSKPIEILDE EGNVKATIRA VWKDSTIYIY
760 770 780 790 800
GEVQDKTKKP AEDGVAIFIN PNNERTPYLQ PDDTYAVLWT NWKTEVNRED
810 820 830 840 850
VQVKKFVGPG FRRYSFEMSI TIPGVEFKKD SYIGFDAAVI DDGKWYSWSD
860 870 880 890 900
TTNSQKTNTM NYGTLKLEGI MVATAKYGTP VIDGEIDEIW NTTEEIETKA
910 920 930 940 950
VAMGSLDKNA TAKVRVLWDE NYLYVLAIVK DPVLNKDNSN PWEQDSVEIF
960 970 980 990 1000
IDENNHKTGY YEDDDAQFRV NYMNEQTFGT GGSPARFKTA VKLIEGGYIV
1010 1020 1030 1040 1050
EAAIKWKTIK PTPNTVIGFN IQVNDANEKG QRVGIISWSD PTNNSWRDPS

KFGNLRLIK
Length:1,059
Mass (Da):119,643
Last modified:November 1, 1997 - v1
Checksum:i045936844A2D72E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46264 Genomic DNA. Translation: CAA86406.1.
AE000512 Genomic DNA. Translation: AAD35155.1.
PIRiS61311.
RefSeqiNP_227877.1. NC_000853.1.
WP_004082550.1. NC_023151.1.
YP_007976409.1. NC_021214.1.
YP_008990963.1. NC_023151.1.

Genome annotation databases

EnsemblBacteriaiAAD35155; AAD35155; TM_0061.
GeneIDi18092750.
896885.
KEGGitma:TM0061.
tmi:THEMA_04500.
PATRICi23934962. VBITheMar51294_0059.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z46264 Genomic DNA. Translation: CAA86406.1.
AE000512 Genomic DNA. Translation: AAD35155.1.
PIRiS61311.
RefSeqiNP_227877.1. NC_000853.1.
WP_004082550.1. NC_023151.1.
YP_007976409.1. NC_021214.1.
YP_008990963.1. NC_023151.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1I82X-ray1.90A871-1059[»]
1I8AX-ray1.90A871-1059[»]
1I8UX-ray1.90A871-1059[»]
ProteinModelPortaliQ60037.
SMRiQ60037. Positions 871-1059.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243274.TM0061.

Protein family/group databases

CAZyiCBM22. Carbohydrate-Binding Module Family 22.
CBM9. Carbohydrate-Binding Module Family 9.
GH10. Glycoside Hydrolase Family 10.

Proteomic databases

PRIDEiQ60037.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35155; AAD35155; TM_0061.
GeneIDi18092750.
896885.
KEGGitma:TM0061.
tmi:THEMA_04500.
PATRICi23934962. VBITheMar51294_0059.

Phylogenomic databases

eggNOGiCOG3693.
InParanoidiQ60037.
KOiK01181.
OMAiQNPTLEF.
OrthoDBiEOG6B363F.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16897.
BRENDAi3.2.1.8. 6331.

Miscellaneous databases

EvolutionaryTraceiQ60037.

Family and domain databases

Gene3Di2.60.120.260. 2 hits.
2.60.40.1190. 2 hits.
3.20.20.80. 1 hit.
InterProiIPR010502. Carb-bd_dom_fam9.
IPR003305. CenC_carb-bd.
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.
PF06452. DUF1083. 2 hits.
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.
PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel cellulose-binding domain within the multidomain 120 kDa xylanase XynA of the hyperthermophilic bacterium Thermotoga maritima."
    Winterhalter C., Heinrich P., Candussio A., Wich G., Liebl W.
    Mol. Microbiol. 15:431-444(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

Entry informationi

Entry nameiXYNA_THEMA
AccessioniPrimary (citable) accession number: Q60037
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: February 4, 2015
This is version 118 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, 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

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 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.