Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P23030

- XYNB_CELJU

UniProt

P23030 - XYNB_CELJU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Endo-1,4-beta-xylanase B

Gene

xynB

Organism
Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Xylanase B contributes to hydrolyze hemicellulose, the major component of plant cell-walls.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei431 – 4311Proton donorBy similarity
Active sitei530 – 5301NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

  1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC
  2. polysaccharide binding Source: InterPro

GO - Biological processi

  1. cellulose catabolic process Source: UniProtKB-KW
  2. xylan catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Cellulose degradation, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

BioCyciCJAP498211:GHIT-3269-MONOMER.
UniPathwayiUPA00697.

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
CBM35. Carbohydrate-Binding Module Family 35.
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
Synonyms:xyn10B
Ordered Locus Names:CJA_3280
OrganismiCellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Taxonomic identifieri498211 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaeCellvibrio
ProteomesiUP000001036: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 37371 PublicationAdd
BLAST
Chaini38 – 599562Endo-1,4-beta-xylanase BPRO_0000007978Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi39 ↔ 133By similarity

Keywords - PTMi

Disulfide bond

Interactioni

Protein-protein interaction databases

STRINGi498211.CJA_3280.

Structurei

3D structure databases

ProteinModelPortaliP23030.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 13699CBM2Add
BLAST
Domaini163 – 289127CBM6PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi135 – 16228Ser-rich (linker)Add
BLAST
Compositional biasi300 – 32021Ser-rich (linker)Add
BLAST

Sequence similaritiesi

Contains 1 CBM6 (carbohydrate binding type-6) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

OrthoDBiEOG6BPDFR.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR005084. CMB_fam6.
IPR008979. Galactose-bd-like.
IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF03422. CBM_6. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00637. CBD_II. 1 hit.
SM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS51175. CBM6. 1 hit.
PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P23030-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTISASDYRH PGNFLKRTTA LLCVGTALTA LAFNASAACT YTIDSEWSTG
60 70 80 90 100
FTANITLKND TGAAINNWNV NWQYSSNRMT SGWNANFSGT NPYNATNMSW
110 120 130 140 150
NGSIAPGQSI SFGLQGEKNG STAERPTVTG AACNSATTSS VASSSSTPTT
160 170 180 190 200
SSSSASSVAS ALLLQEAQAG FCRVDGTIDN NHTGFTGSGF ANTNNAQGAA
210 220 230 240 250
VVWAIDATSS GRRTLTIRYA NGGTANRNGS LVINGGSNGN YTVSLPTTGA
260 270 280 290 300
WTTWQTATID VDLVQGNNIV QLSATTAEGL PNIDSLSVVG GTVRAGNCGS
310 320 330 340 350
VSSSSSVQSS SSSSSSSAAS AKKFIGNITT SGAVRSDFTR YWNQITPENE
360 370 380 390 400
SKWGSVEGTR NVYNWAPLDR IYAYARQNNI PVKAHTFVWG AQSPSWLNNL
410 420 430 440 450
SGPEVAVEIE QWIRDYCARY PDTAMIDVVN EAVPGHQPAG YAQRAFGNNW
460 470 480 490 500
IQRVFQLARQ YCPNSILILN DYNNIRWQHN EFIALAKAQG NYIDAVGLQA
510 520 530 540 550
HELKGMTAAQ VKTAIDNIWN QVGKPIYISE YDIGDTNDQV QLQNFQAHFP
560 570 580 590
VFYNHPHVHG ITLWGYVVGR TWIEGSGLIQ DNGTPRPAMT WLINNYLNQ
Length:599
Mass (Da):64,363
Last modified:April 20, 2010 - v2
Checksum:iD2DE51E5FD4B33E5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti563 – 59836LWGYV…NNYLN → SGICGGQDLDRRLRFDPGQW HTAPGNDVVD in CAA38389. (PubMed:2125205)CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54523 Genomic DNA. Translation: CAA38389.1.
CP000934 Genomic DNA. Translation: ACE84499.1.
RefSeqiYP_001983734.1. NC_010995.1.

Genome annotation databases

EnsemblBacteriaiACE84499; ACE84499; CJA_3280.
GeneIDi6416364.
KEGGicja:CJA_3280.
PATRICi21329951. VBICelJap122165_3240.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X54523 Genomic DNA. Translation: CAA38389.1 .
CP000934 Genomic DNA. Translation: ACE84499.1 .
RefSeqi YP_001983734.1. NC_010995.1.

3D structure databases

ProteinModelPortali P23030.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 498211.CJA_3280.

Protein family/group databases

CAZyi CBM2. Carbohydrate-Binding Module Family 2.
CBM35. Carbohydrate-Binding Module Family 35.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai ACE84499 ; ACE84499 ; CJA_3280 .
GeneIDi 6416364.
KEGGi cja:CJA_3280.
PATRICi 21329951. VBICelJap122165_3240.

Phylogenomic databases

OrthoDBi EOG6BPDFR.

Enzyme and pathway databases

UniPathwayi UPA00697 .
BioCyci CJAP498211:GHIT-3269-MONOMER.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProi IPR008965. Carb-bd_dom.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001919. Cellulose-bd_dom_fam2_bac.
IPR005084. CMB_fam6.
IPR008979. Galactose-bd-like.
IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00553. CBM_2. 1 hit.
PF03422. CBM_6. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view ]
PRINTSi PR00134. GLHYDRLASE10.
SMARTi SM00637. CBD_II. 1 hit.
SM00633. Glyco_10. 1 hit.
[Graphical view ]
SUPFAMi SSF49384. SSF49384. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEi PS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS51175. CBM6. 1 hit.
PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Xylanase B and an arabinofuranosidase from Pseudomonas fluorescens subsp. cellulosa contain identical cellulose-binding domains and are encoded by adjacent genes."
    Kellett L.E., Poole D.M., Ferreira L.M.A., Durrant A.J., Hazlewood G.P., Gilbert H.J.
    Biochem. J. 272:369-376(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 38-46.
  2. "Insights into plant cell wall degradation from the genome sequence of the soil bacterium Cellvibrio japonicus."
    DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H., Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J., Nelson K.E.
    J. Bacteriol. 190:5455-5463(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ueda107.

Entry informationi

Entry nameiXYNB_CELJU
AccessioniPrimary (citable) accession number: P23030
Secondary accession number(s): B3PEH8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: April 20, 2010
Last modified: October 1, 2014
This is version 99 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

Complete proteome, Direct protein sequencing, Reference proteome

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