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Protein

Bifunctional endo-1,4-beta-xylanase XylA

Gene

xynA

Organism
Ruminococcus flavefaciens
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Xylanase domain 1 releases more xylo-oligosaccharides and domain 2 more xylose.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei122 – 1221NucleophileBy similarity
Active sitei223 – 2231Proton donorPROSITE-ProRule annotation
Active sitei774 – 7741Proton donorPROSITE-ProRule annotation
Active sitei884 – 8841NucleophileBy similarity

GO - Molecular functioni

  1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-UniPathway
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

CAZyiGH10. Glycoside Hydrolase Family 10.
GH11. Glycoside Hydrolase Family 11.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional endo-1,4-beta-xylanase XylA (EC:3.2.1.8)
Gene namesi
Name:xynA
OrganismiRuminococcus flavefaciens
Taxonomic identifieri1265 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Or 28, or 29Sequence AnalysisAdd
BLAST
Chaini28 – 954927Bifunctional endo-1,4-beta-xylanase XylAPRO_0000008015Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP29126.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni28 – 244217Xylanase domain 1Add
BLAST
Regioni623 – 954332Xylanase domain 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi245 – 622378Asn/Gln/Trp-rich (linker)Add
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the glycosyl hydrolase 11 (cellulase G) family.Curated
In the C-terminal section; belongs to the glycosyl hydrolase 10 (cellulase F) family.Curated

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001000. Glyco_hydro_10.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
PF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P29126-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLSKIKKVL SGTVSALMIA SAAPVVASAA DQQTRGNVGG YDYEMWNQNG
60 70 80 90 100
QGQASMNPGA GSFTCSWSNI ENFLARMGKN YDSQKKNYKA FGNIVLTYDV
110 120 130 140 150
EYTPRGNSYM CVYGWTRNPL MEYYIVEGWG DWRPPGNDGE VKGTVSANGN
160 170 180 190 200
TYDIRKTMRY NQPSLDGTAT FPQYWSVRQT SGSANNQTNY MKGTIDVTKH
210 220 230 240 250
FDAWSAAGLD MSGTLYEVSL NIEGYRSNGS ANVKSVSVTQ GGSSDNGGQQ
260 270 280 290 300
QNNDWNQQNN NQQQNNDWNN WGQQNNDWNQ WNNQGQQNND WNNWGQQNND
310 320 330 340 350
WNQWNNQGQQ QNNDWNNWGQ QNNDWNQWNN QGQQQNNDWN NWGQQNNDWN
360 370 380 390 400
QWNNQGQQQN NDWNNWGQQN NDWNQWNNQN NNQQNAWNGW DNNNNWNQNN
410 420 430 440 450
QQQNNWDWNN QNNWNNNQQQ NNDWNQWNNQ NNWNNNQQQN NDWNQWNNQG
460 470 480 490 500
QQNNDWNQWN NQNNWNQNNN QQNAWNGWDN NNNWNQWDQN NQWNNQQQNN
510 520 530 540 550
TWDWNNQNNW NNNQQNNDWN QWNNQGQQQN NDWNQWNNQN NNQNNGWDWN
560 570 580 590 600
NQNNWNQNNN QQNAWNGWDN NNNWNQWGGQ NNDWNNQQQN NDWNQWNNQG
610 620 630 640 650
QQQNNDWNNQ NNWNQGQQNN NNSAGSSDSL KGAFSKYFKI GTSVSPHELN
660 670 680 690 700
SGADFLKKHY NSITPENELK PESILDQGAC QQKGNNVNTQ ISLSRAAQTL
710 720 730 740 750
KFCEQNGIAL RGHTFVWYSQ TPDWFFRENF SQNGAYVSKD IMNQRLESMI
760 770 780 790 800
KNTFAALKSQ YPNLDVYSYD VCNELFLNNG GGMRGADNSN WVKIYGDDSF
810 820 830 840 850
VINAFKYARQ YAPAGCKLYL NDYNEYIPAK TNDIYNMAMK LKQLGYIDGI
860 870 880 890 900
GMQSHLATNY PDANTYETAL KKFLSTGLEV QITELDITCT NSAEQADLYE
910 920 930 940 950
KIFKLAMQNS AQIPAVTIWG TQDTVSWRSS QNPLLFSAGY QPKPAYDRVM

ALAK
Length:954
Mass (Da):111,362
Last modified:December 1, 1992 - v1
Checksum:i1033567D4B526EBD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11127 Genomic DNA. Translation: CAA77476.1.
PIRiS20907.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z11127 Genomic DNA. Translation: CAA77476.1.
PIRiS20907.

3D structure databases

ProteinModelPortaliP29126.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH10. Glycoside Hydrolase Family 10.
GH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR013320. ConA-like_dom.
IPR001000. Glyco_hydro_10.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
PF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A bifunctional xylanase encoded by the xynA gene of the rumen cellulolytic bacterium Ruminococcus flavefaciens 17 comprises two dissimilar domains linked by an asparagine/glutamine-rich sequence."
    Zhang J.-X., Flint H.J.
    Mol. Microbiol. 6:1013-1023(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 17.

Entry informationi

Entry nameiXYNA_RUMFL
AccessioniPrimary (citable) accession number: P29126
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: October 29, 2014
This is version 78 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

Multifunctional enzyme

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

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.