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Protein

Bifunctional xylanase/xylan deacetylase

Gene

xyn11A

Organism
Cellvibrio japonicus (Pseudomonas fluorescens subsp. cellulosa)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Endo-acting xylanase which specifically cleaves internal linkages on the xylan backbone, releasing xylooligosaccharides. Is able to hydrolyze oat spelt xylan and the arabinoxylans from wheat and rye, releasing xylobiose as the major product. Also likely catalyzes, via its C-terminal domain, the removal of acetyl groups from acetylated xylan. Thus, has the capability of hydrolyzing acetylated xylan. Does not attack mannan, galactan, arabinan or any cellulosic substrates.2 Publications

Catalytic activityi

Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.1 Publication
Deacetylation of xylans and xylo-oligosaccharides.1 Publication

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 sitei116 – 1161Nucleophile; for endoxylanase activityPROSITE-ProRule annotation
Active sitei213 – 2131Proton donor; for endoxylanase activityBy 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

SABIO-RKQ59674.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM10. Carbohydrate-Binding Module Family 10.
GH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11E_CELJA.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional xylanase/xylan deacetylase
Alternative name(s):
XYLE
Including the following 2 domains:
Endo-1,4-beta-xylanase Xyn11A (EC:3.2.1.8)
Short name:
Xylanase 11A
Acetylxylan deacetylase (EC:3.1.1.72)
Gene namesi
Name:xyn11A
Synonyms:xynE
OrganismiCellvibrio japonicus (Pseudomonas fluorescens subsp. cellulosa)
Taxonomic identifieri155077 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaCellvibrionalesCellvibrionaceaeCellvibrio

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Sequence analysisAdd
BLAST
Chaini28 – 661634Bifunctional xylanase/xylan deacetylasePRO_5000147608Add
BLAST

Expressioni

Inductioni

Induced when the bacterium is cultured on xylan or beta-glucan but not on medium containing mannan. Is repressed by glucose. Transcription of xyn11A occurs in early exponential phase, and thus earlier than transcription of xyn11B.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi498211.CJA_3763.

Structurei

3D structure databases

ProteinModelPortaliQ59674.
SMRiQ59674. Positions 395-586, 613-651.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini29 – 226198GH11PROSITE-ProRule annotationAdd
BLAST
Domaini398 – 574177NodB homologyPROSITE-ProRule annotationAdd
BLAST
Domaini616 – 64530CBM10PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni394 – 577184Polysaccharide deacetylaseAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi228 – 401174Gly-richAdd
BLAST
Compositional biasi587 – 60620Ser-richAdd
BLAST

Domaini

The N-terminal domain possesses xylanase activity, the central region likely has xylan deacetylase activity, and the small C-terminal domain is involved in carbohydrate-binding.1 Publication

Sequence similaritiesi

In the N-terminal section; belongs to the glycosyl hydrolase 11 (cellulase G) family.Curated
Contains 1 CBM10 (carbohydrate binding type-10) domain.PROSITE-ProRule annotationCurated
Contains 1 GH11 (glycosyl hydrolase family 11) domain.PROSITE-ProRule annotation
Contains 1 NodB homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108ZJ4. Bacteria.
COG0726. LUCA.

Family and domain databases

Gene3Di2.30.32.30. 1 hit.
2.60.120.180. 1 hit.
3.20.20.370. 1 hit.
InterProiIPR002883. CBM10/Dockerin_dom.
IPR031768. CBM60_xylan-bd.
IPR009031. CBM_fam10.
IPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033123. GH11_dom.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR001137. Glyco_hydro_11.
IPR002509. NODB_dom.
[Graphical view]
PfamiPF16841. CBM60. 1 hit.
PF02013. CBM_10. 1 hit.
PF00457. Glyco_hydro_11. 1 hit.
PF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SMARTiSM01064. CBM_10. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF57615. SSF57615. 1 hit.
SSF88713. SSF88713. 1 hit.
PROSITEiPS51763. CBM10. 1 hit.
PS00776. GH11_1. 1 hit.
PS51761. GH11_3. 1 hit.
PS51677. NODB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q59674-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLPTLGKCV VRTLMGAVAL GAISVNAQTL SSNSTGTNNG FYYTFWKDSG
60 70 80 90 100
DASMTLLSGG RYQSSWGNST NNWVGGKGWN PGNNSRVISY SGSYGVDSSQ
110 120 130 140 150
NSYLALYGWT RSPLIEYYVI ESYGSYNPAS CSGGTDYGSF QSDGATYNVR
160 170 180 190 200
RCQRVNQPSI DGTQTFYQYF SVRNPKKGFG NISGTITFAN HVNFWASKGL
210 220 230 240 250
NLGNHNYQVL ATEGYQSRGS SDITVSEGTS GGGTSSVGGA SSSVNSSTGG
260 270 280 290 300
GSSGGITVRA RGANGSEHIN LRVGGAVVAN WTLGTSFQNY LYSGNASGDI
310 320 330 340 350
QVQFDNDASG RDVVVDYIIV NGETRQAEDM EHNSAVYANG RCGGGSYSEN
360 370 380 390 400
MHCNGEIGFG YTYDCFSGNC SGGNGGSNSS AGNSSSGNTG GGGSNCSGYV
410 420 430 440 450
GITFDDGPNS NTATLVNLLR QNNLTPVTWF NQGNNVASNA HLMSQQLSVG
460 470 480 490 500
EVHNHSYTHP HMTSWTYQQV YDELNRTNQA IQNAGAPKPT LFRPPYGELN
510 520 530 540 550
STIQQAAQAL GLRVVTWDVD SQDWNGASAA AIANAANQLQ NGQVILMHDG
560 570 580 590 600
SYTNTNSAIA QIATNLRAKG LCPGRIDPNT GRAVAPSSSG GSSSVALSSS
610 620 630 640 650
SRSSSSAGGN TGGNCQCNWW GTFYPLCQTQ TSGWGWENSR SCISTSTCNS
660
QGTGGGGVVC N
Length:661
Mass (Da):69,193
Last modified:November 1, 1996 - v1
Checksum:i3D8C897D4C732FEB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48927 Genomic DNA. Translation: CAA88763.1.
PIRiS59633.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48927 Genomic DNA. Translation: CAA88763.1.
PIRiS59633.

3D structure databases

ProteinModelPortaliQ59674.
SMRiQ59674. Positions 395-586, 613-651.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi498211.CJA_3763.

Protein family/group databases

CAZyiCBM10. Carbohydrate-Binding Module Family 10.
GH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11E_CELJA.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108ZJ4. Bacteria.
COG0726. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00114.
SABIO-RKQ59674.

Family and domain databases

Gene3Di2.30.32.30. 1 hit.
2.60.120.180. 1 hit.
3.20.20.370. 1 hit.
InterProiIPR002883. CBM10/Dockerin_dom.
IPR031768. CBM60_xylan-bd.
IPR009031. CBM_fam10.
IPR013320. ConA-like_dom.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033123. GH11_dom.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR001137. Glyco_hydro_11.
IPR002509. NODB_dom.
[Graphical view]
PfamiPF16841. CBM60. 1 hit.
PF02013. CBM_10. 1 hit.
PF00457. Glyco_hydro_11. 1 hit.
PF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SMARTiSM01064. CBM_10. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 1 hit.
SSF57615. SSF57615. 1 hit.
SSF88713. SSF88713. 1 hit.
PROSITEiPS51763. CBM10. 1 hit.
PS00776. GH11_1. 1 hit.
PS51761. GH11_3. 1 hit.
PS51677. NODB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Novel cellulose-binding domains, NodB homologues and conserved modular architecture in xylanases from the aerobic soil bacteria Pseudomonas fluorescens subsp. cellulosa and Cellvibrio mixtus."
    Millward-Sadler S.J., Davidson K., Hazlewood G.P., Black G.W., Gilbert H.J., Clarke J.H.
    Biochem. J. 312:39-48(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION AS A XYLANASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, DOMAIN.
    Strain: NCIMB 10462.
  2. "Evidence for temporal regulation of the two Pseudomonas cellulosa xylanases belonging to glycoside hydrolase family 11."
    Emami K., Nagy T., Fontes C.M., Ferreira L.M., Gilbert H.J.
    J. Bacteriol. 184:4124-4133(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION.

Entry informationi

Entry nameiXY11A_CELJA
AccessioniPrimary (citable) accession number: Q59674
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 11, 2013
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 77 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.