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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)DescriptionActionsGraphical viewLength
Active sitei144Proton donorBy similarity1
Active sitei255NucleophilePROSITE-ProRule annotation1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Sequence analysisAdd BLAST20
ChainiPRO_000042966621 – 860Endo-1,4-beta-xylanase BAdd BLAST840

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi278 ↔ 284By similarity
Glycosylationi295N-linked (GlcNAc...)Sequence analysis1
Glycosylationi309N-linked (GlcNAc...)Sequence analysis1
Glycosylationi359N-linked (GlcNAc...)Sequence analysis1
Glycosylationi374N-linked (GlcNAc...)Sequence analysis1
Glycosylationi390N-linked (GlcNAc...)Sequence analysis1
Glycosylationi406N-linked (GlcNAc...)Sequence analysis1
Glycosylationi845N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ02290.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini21 – 324GH10PROSITE-ProRule annotationAdd BLAST304
Repeati375 – 38218
Repeati391 – 39828
Repeati415 – 42238
Repeati431 – 43848
Repeati439 – 44658
Repeati447 – 45468
Repeati455 – 46278
Repeati463 – 47088
Repeati471 – 47898
Repeati479 – 486108
Repeati487 – 494118
Repeati495 – 502128
Repeati503 – 510138
Repeati511 – 518148
Repeati519 – 526158
Repeati527 – 534168
Repeati535 – 542178
Repeati543 – 550188
Repeati551 – 558198
Repeati559 – 566208
Repeati567 – 574218
Repeati575 – 582228
Repeati583 – 590238
Repeati591 – 598248
Repeati599 – 606258
Repeati607 – 614268
Repeati615 – 622278
Repeati623 – 630288
Repeati631 – 638298
Repeati639 – 646308
Repeati647 – 654318
Repeati655 – 662328
Repeati663 – 670338
Repeati671 – 678348
Repeati679 – 686358
Repeati687 – 694368
Repeati695 – 702378
Repeati703 – 710388
Repeati711 – 718398
Repeati719 – 726408
Repeati727 – 734418
Repeati735 – 742428
Repeati743 – 750438
Repeati751 – 758448
Repeati759 – 766458
Repeati767 – 774468
Repeati775 – 782478
Domaini824 – 860CBM1PROSITE-ProRule annotationAdd BLAST37

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni375 – 78247 X 8 AA tandem repeats of [SKN]-S-K-T-L-P-G-GAdd BLAST408

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.
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...

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: October 5, 2016
This is version 74 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.