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Protein

Endo-1,4-beta-xylanase B

Gene

xynB

Organism
Neocallimastix patriciarum (Rumen fungus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose. Hydrolyzes both unsubstituted (oat spelts) and highly substituted (rye and wheat) forms of arabinoxylanslans.

Catalytic activityi

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

Pathwayi: xylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei144 – 1441Proton donorBy similarity
Active sitei255 – 2551NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH10. Glycoside Hydrolase Family 10.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase B (EC:3.2.1.8)
Short name:
Xylanase B
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase B
Gene namesi
Name:xynB
OrganismiNeocallimastix patriciarum (Rumen fungus)
Taxonomic identifieri4758 [NCBI]
Taxonomic lineageiEukaryotaFungiNeocallimastigomycotaNeocallimastigomycetesNeocallimastigalesNeocallimastigaceaeNeocallimastix

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Sequence analysisAdd
BLAST
Chaini21 – 860840Endo-1,4-beta-xylanase BPRO_0000429666Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi278 ↔ 284By similarity
Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence analysis
Glycosylationi309 – 3091N-linked (GlcNAc...)Sequence analysis
Glycosylationi359 – 3591N-linked (GlcNAc...)Sequence analysis
Glycosylationi374 – 3741N-linked (GlcNAc...)Sequence analysis
Glycosylationi390 – 3901N-linked (GlcNAc...)Sequence analysis
Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence analysis
Glycosylationi845 – 8451N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ02290.
SMRiQ02290. Positions 826-860.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 324304GH10PROSITE-ProRule annotationAdd
BLAST
Repeati375 – 38281
Repeati391 – 39882
Repeati415 – 42283
Repeati431 – 43884
Repeati439 – 44685
Repeati447 – 45486
Repeati455 – 46287
Repeati463 – 47088
Repeati471 – 47889
Repeati479 – 486810
Repeati487 – 494811
Repeati495 – 502812
Repeati503 – 510813
Repeati511 – 518814
Repeati519 – 526815
Repeati527 – 534816
Repeati535 – 542817
Repeati543 – 550818
Repeati551 – 558819
Repeati559 – 566820
Repeati567 – 574821
Repeati575 – 582822
Repeati583 – 590823
Repeati591 – 598824
Repeati599 – 606825
Repeati607 – 614826
Repeati615 – 622827
Repeati623 – 630828
Repeati631 – 638829
Repeati639 – 646830
Repeati647 – 654831
Repeati655 – 662832
Repeati663 – 670833
Repeati671 – 678834
Repeati679 – 686835
Repeati687 – 694836
Repeati695 – 702837
Repeati703 – 710838
Repeati711 – 718839
Repeati719 – 726840
Repeati727 – 734841
Repeati735 – 742842
Repeati743 – 750843
Repeati751 – 758844
Repeati759 – 766845
Repeati767 – 774846
Repeati775 – 782847
Domaini824 – 86037CBM1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni375 – 78240847 X 8 AA tandem repeats of [SKN]-S-K-T-L-P-G-GAdd
BLAST

Sequence similaritiesi

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.PROSITE-ProRule annotation
Contains 1 GH10 (glycosyl hydrolase family 10) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR001000. GH10.
IPR031158. GH10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
SM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
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.

Q02290-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFSSANKIL FSGLVASANA YDLLKDYAGD LKIGVAANAM RFSNSNYVNA
60 70 80 90 100
MKAFNMMVAE NDCKLSGIQQ QKGVYNFNGC DNHYNKAKEL GMEFRGHCLI
110 120 130 140 150
WHSYQPSWFQ NADANTLKNA IVDHITKTLQ HYEGKIKVWD VVNEAIDDNS
160 170 180 190 200
NGNGWNMRRS FLYNKVPNFV DLAFQTARKV SPNTKLFYND YNAEGVYAKA
210 220 230 240 250
ESIYNFVSDL KKRNIPIDGV GLQYHVGAKE QPSYNKINDL IGRYCKLGLE
260 270 280 290 300
VHITELDVKL QGDQNGQSQA FSNALKACLA NSCCKAFLVW GVGDNDSWLG
310 320 330 340 350
ANEQALLFNG SYQPKPVYNT LLNILKTSAR PASSSAKTLP GNSKSKTLPG
360 370 380 390 400
VNSKTLPGNK SKTLPGASKT LPGNKSKTLP GGNSNTLPGN KSKTLPGGNS
410 420 430 440 450
KTLPGNKSRT LPGGNSKTLP GGKSRTLPGG NSKTLPGGKS KTLPGGNSKT
460 470 480 490 500
LPGGKSKTLP GGNSKTLPGG SSKTLPGGKS KTLPGGNSKT LPGGSSKTLP
510 520 530 540 550
GGKSKTLPGG SSKTLPGGKS KTLPGGNSKT LPGGNSKTLP GGSSKTLPGG
560 570 580 590 600
KSKTLPGGNS KTLPGGSSKT LPGGKSKTLP GGNSKTLPGG NSKTLPGGKS
610 620 630 640 650
KTLPGGNSKT LPGGSSKTLP GGKSKTLPGG SSKTLPGGKS KTLPGGNSKT
660 670 680 690 700
LPGGNSKTLP GGSSKTLPGG KSKTLPGGSS KTLPGGKSKT LPGGNSKTLP
710 720 730 740 750
GGKSKTLPGG NSKTLPGGKS KTLPGGNSKT LPGGKSKTLP GGNSKTLPGG
760 770 780 790 800
SSKTLPGGKS KTLPGGNSKT LPGGKSKTLP GGNTKTLPGG ACKPTTVTVT
810 820 830 840 850
QKVTVTVTVE SQPTQGGMNQ GGGNCAAKWG QCGGNGFNGP TCCQNGSRCQ
860
FVNEWYSQCL
Length:860
Mass (Da):88,052
Last modified:November 1, 1996 - v1
Checksum:i677F9032F0A87085
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S71569 mRNA. Translation: AAB30669.1.
PIRiS43846.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S71569 mRNA. Translation: AAB30669.1.
PIRiS43846.

3D structure databases

ProteinModelPortaliQ02290.
SMRiQ02290. Positions 826-860.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM1. Carbohydrate-Binding Module Family 1.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR000254. Cellulose-bd_dom_fun.
IPR001000. GH10.
IPR031158. GH10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00734. CBM_1. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
ProDomiPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00236. fCBD. 1 hit.
SM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEiPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00591. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Xylanase B from Neocallimastix patriciarum contains a non-catalytic 455-residue linker sequence comprised of 57 repeats of an octapeptide."
    Black G.W., Hazlewood G.P., Xue G.P., Orpin C.G., Gilbert H.J.
    Biochem. J. 299:381-387(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiXYNB_NEOPA
AccessioniPrimary (citable) accession number: Q02290
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 9, 2014
Last sequence update: November 1, 1996
Last modified: March 16, 2016
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.