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Protein

Bifunctional xylanase/xylan deacetylase

Gene

xyn11A

Organism
Cellvibrio japonicus (Pseudomonas fluorescens subsp. cellulosa)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Active sitei116Nucleophile; for endoxylanase activityPROSITE-ProRule annotation1
Active sitei213Proton donor; for endoxylanase activityBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase, Multifunctional enzyme
Biological processCarbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

SABIO-RKiQ59674
UniPathwayi
UPA00114

Protein family/group databases

CAZyiCBM10 Carbohydrate-Binding Module Family 10
CBM60 Carbohydrate-Binding Module Family 60
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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 27Sequence analysisAdd BLAST27
ChainiPRO_500014760828 – 661Bifunctional xylanase/xylan deacetylaseAdd BLAST634

Proteomic databases

PRIDEiQ59674

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

Structurei

3D structure databases

ProteinModelPortaliQ59674
SMRiQ59674
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 226GH11PROSITE-ProRule annotationAdd BLAST198
Domaini398 – 574NodB homologyPROSITE-ProRule annotationAdd BLAST177
Domaini616 – 645CBM10PROSITE-ProRule annotationAdd BLAST30

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni394 – 577Polysaccharide deacetylaseAdd BLAST184

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi228 – 401Gly-richAdd BLAST174
Compositional biasi587 – 606Ser-richAdd BLAST20

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

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
InterProiView protein in InterPro
IPR002883 CBM10/Dockerin_dom
IPR036601 CBM10_sf
IPR031768 CBM60_xylan-bd
IPR009031 CBM_fam10
IPR013320 ConA-like_dom_sf
IPR013319 GH11/12
IPR018208 GH11_AS_1
IPR033123 GH11_dom
IPR011330 Glyco_hydro/deAcase_b/a-brl
IPR001137 Glyco_hydro_11
IPR002509 NODB_dom
PfamiView protein in Pfam
PF16841 CBM60, 1 hit
PF02013 CBM_10, 1 hit
PF00457 Glyco_hydro_11, 1 hit
PF01522 Polysacc_deac_1, 1 hit
PRINTSiPR00911 GLHYDRLASE11
SMARTiView protein in SMART
SM01064 CBM_10, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit
SSF57615 SSF57615, 1 hit
SSF88713 SSF88713, 1 hit
PROSITEiView protein in PROSITE
PS51763 CBM10, 1 hit
PS00776 GH11_1, 1 hit
PS51761 GH11_3, 1 hit
PS51677 NODB, 1 hit

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

Similar proteinsi

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
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM10 Carbohydrate-Binding Module Family 10
CBM60 Carbohydrate-Binding Module Family 60
GH11 Glycoside Hydrolase Family 11
mycoCLAPiXYN11E_CELJA

Proteomic databases

PRIDEiQ59674

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108ZJ4 Bacteria
COG0726 LUCA

Enzyme and pathway databases

UniPathwayi
UPA00114

SABIO-RKiQ59674

Family and domain databases

Gene3Di2.30.32.30, 1 hit
2.60.120.180, 1 hit
InterProiView protein in InterPro
IPR002883 CBM10/Dockerin_dom
IPR036601 CBM10_sf
IPR031768 CBM60_xylan-bd
IPR009031 CBM_fam10
IPR013320 ConA-like_dom_sf
IPR013319 GH11/12
IPR018208 GH11_AS_1
IPR033123 GH11_dom
IPR011330 Glyco_hydro/deAcase_b/a-brl
IPR001137 Glyco_hydro_11
IPR002509 NODB_dom
PfamiView protein in Pfam
PF16841 CBM60, 1 hit
PF02013 CBM_10, 1 hit
PF00457 Glyco_hydro_11, 1 hit
PF01522 Polysacc_deac_1, 1 hit
PRINTSiPR00911 GLHYDRLASE11
SMARTiView protein in SMART
SM01064 CBM_10, 1 hit
SUPFAMiSSF49899 SSF49899, 1 hit
SSF57615 SSF57615, 1 hit
SSF88713 SSF88713, 1 hit
PROSITEiView protein in PROSITE
PS51763 CBM10, 1 hit
PS00776 GH11_1, 1 hit
PS51761 GH11_3, 1 hit
PS51677 NODB, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiXY11A_CELJA
AccessioniPrimary (citable) accession number: Q59674
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 11, 2013
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 86 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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Main funding by: National Institutes of Health

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