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Protein

Xylanase/beta-glucanase

Gene

xynD

Organism
Ruminococcus flavefaciens
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Contains two catalytic domains with xylanase and endo-beta-1,3-1,4 glucanase activities.

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.

Pathway: 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 sitei124 – 1241NucleophileBy similarity
Active sitei226 – 2261Proton donorPROSITE-ProRule annotation
Active sitei684 – 6841NucleophileBy similarity

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

CAZyiCBM22. Carbohydrate-Binding Module Family 22.
GH11. Glycoside Hydrolase Family 11.
GH16. Glycoside Hydrolase Family 16.
mycoCLAPiZXG11D_RUMFL.

Names & Taxonomyi

Protein namesi
Recommended name:
Xylanase/beta-glucanase
Including the following 2 domains:
Endo-1,4-beta-xylanase (EC:3.2.1.8)
Short name:
Xylanase
Endo-beta-1,3-1,4 glucanase (EC:3.2.1.73)
Alternative name(s):
1,3-1,4-beta-D-glucan 4-glucanohydrolase
Lichenase
Gene namesi
Name:xynD
OrganismiRuminococcus flavefaciens
Taxonomic identifieri1265 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminococcus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Chaini32 – 802771Xylanase/beta-glucanasePRO_0000008009Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ53317.
SMRiQ53317. Positions 575-790.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini258 – 404147CBM-cenCAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni32 – 244213A (xylanase)Add
BLAST
Regioni245 – 523279BAdd
BLAST
Regioni524 – 55532LinkerAdd
BLAST
Regioni556 – 802247C (beta-glucanase)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi524 – 5296Poly-Thr
Compositional biasi532 – 54312Poly-ThrAdd
BLAST
Compositional biasi546 – 5538Poly-Thr

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 16 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
2.60.120.180. 1 hit.
2.60.120.200. 1 hit.
2.60.120.260. 1 hit.
InterProiIPR008264. Beta_glucanase.
IPR016134. Cellulos_enz_dockerin_1.
IPR003305. CenC_carb-bd.
IPR013320. ConA-like_dom.
IPR008979. Galactose-bd-like.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
IPR000757. Glyco_hydro_16.
IPR008263. Glycoside_hydrolase_16_AS.
[Graphical view]
PfamiPF02018. CBM_4_9. 1 hit.
PF00457. Glyco_hydro_11. 1 hit.
PF00722. Glyco_hydro_16. 1 hit.
[Graphical view]
PRINTSiPR00737. GLHYDRLASE16.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 2 hits.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
PS01034. GLYCOSYL_HYDROL_F16. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q53317-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKSIFKRYA AAVGLMASVL MFTAVPTTSN AADDQKTGKV GGFDWEMWNQ
60 70 80 90 100
NYTGTVSMNP GAGSFTCSWS GIENFLARMG KNYDDQKKNY KAFGDIVLTY
110 120 130 140 150
DVEYTPRGNS YMCIYGWTRN PLMEYYIVEG WGDWEPPGND GVDNFGTTTI
160 170 180 190 200
DGKTYKIRKS MRYNQPSIEG TKTFPQYWSV RTTSGSRNNT TNYMKDQVSV
210 220 230 240 250
TKHFDAWSKA GLDMSGTLYE VSLNIEGYRS NGSANVKSIS FDGGIDIPDP
260 270 280 290 300
EPIKPDENGY YLKENFESGE GNWSGRGSAK VKSSSGYDGT KGIFVSGRED
310 320 330 340 350
TWNGASINLD ELTFKAGETY SLGTAVMQDF ESSVDFKLTL QYTDADGKEN
360 370 380 390 400
YDEVKTVTAA KGQWVDLSNS SYTIPSGATG LVLYVEVPES KTDFYMDGAY
410 420 430 440 450
AGVKGTKPLI SISSQSVDPP VTEPTNPTNP TGPSVTKWGD ANCDGGVDLS
460 470 480 490 500
DAIFIMQFLA NPNKYGLTGT ETNHMTNQGK VNGDVCEHGS GLTEDDAVSI
510 520 530 540 550
QKYLIRAISE LPESYLEGHD PSKTTTTTTR ITTTTTTTTT TTTSKTTTTT
560 570 580 590 600
TTTSPAMHGG YRDLGTPMNT SATMISDFRT GKAGDFFASD GWTNGKPFDC
610 620 630 640 650
WWYKRNAVIN DGCLQLSIDQ KWTNDKNPDW DPRYSGGEFR TNNFYHYGYY
660 670 680 690 700
ECSMQAMKND GVVSSFFTYT GPSDDNPWDE IDIEILGKNT TQVQFNYYTN
710 720 730 740 750
GQGKHEKLYD LGFDSSEAYH TYGFDWQPNY IAWYVDGREV YRATQDIPKT
760 770 780 790 800
PGKIMMNAWP GLTVDDWLKA FNGRTPLTAH YQWVTYNKNG VQHSSQGQNP

WG
Length:802
Mass (Da):89,091
Last modified:November 1, 1997 - v2
Checksum:i2880A689647284AF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S61204 Genomic DNA. Translation: AAB26620.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S61204 Genomic DNA. Translation: AAB26620.1.

3D structure databases

ProteinModelPortaliQ53317.
SMRiQ53317. Positions 575-790.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM22. Carbohydrate-Binding Module Family 22.
GH11. Glycoside Hydrolase Family 11.
GH16. Glycoside Hydrolase Family 16.
mycoCLAPiZXG11D_RUMFL.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.

Family and domain databases

Gene3Di1.10.1330.10. 1 hit.
2.60.120.180. 1 hit.
2.60.120.200. 1 hit.
2.60.120.260. 1 hit.
InterProiIPR008264. Beta_glucanase.
IPR016134. Cellulos_enz_dockerin_1.
IPR003305. CenC_carb-bd.
IPR013320. ConA-like_dom.
IPR008979. Galactose-bd-like.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
IPR000757. Glyco_hydro_16.
IPR008263. Glycoside_hydrolase_16_AS.
[Graphical view]
PfamiPF02018. CBM_4_9. 1 hit.
PF00457. Glyco_hydro_11. 1 hit.
PF00722. Glyco_hydro_16. 1 hit.
[Graphical view]
PRINTSiPR00737. GLHYDRLASE16.
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 2 hits.
SSF63446. SSF63446. 1 hit.
PROSITEiPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
PS01034. GLYCOSYL_HYDROL_F16. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "A bifunctional enzyme, with separate xylanase and beta(1,3-1,4)-glucanase domains, encoded by the xynD gene of Ruminococcus flavefaciens."
    Flint H.J., Martin J., McPherson C.A., Daniel A.S., Zhang J.-X.
    J. Bacteriol. 175:2943-2951(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 17.

Entry informationi

Entry nameiXYND_RUMFL
AccessioniPrimary (citable) accession number: Q53317
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 29, 2015
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.