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P00694

- XYNA_BACPU

UniProt

P00694 - XYNA_BACPU

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Protein

Endo-1,4-beta-xylanase A

Gene
xynA
Organism
Bacillus pumilus (Bacillus mesentericus)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei120 – 1201Nucleophile By similarity
Active sitei209 – 2091Proton donor By 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

CAZyiGH11. Glycoside Hydrolase Family 11.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase A (EC:3.2.1.8)
Short name:
Xylanase A
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase A
Gene namesi
Name:xynA
OrganismiBacillus pumilus (Bacillus mesentericus)
Taxonomic identifieri1408 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi120 – 1201E → S: Loss of activity.
Mutagenesisi209 – 2091E → D: Loss of activity.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727Add
BLAST
Chaini28 – 228201Endo-1,4-beta-xylanase APRO_0000007997Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP00694.
SMRiP00694. Positions 27-227.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR008985. ConA-like_lec_gl_sf.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamiPF00457. Glyco_hydro_11. 1 hit.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 1 hit.
PROSITEiPS00776. 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.

P00694-1 [UniParc]FASTAAdd to Basket

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MNLRKLRLLF VMCIGLTLIL TAVPAHARTI TNNEMGNHSG YDYELWKDYG    50
NTSMTLNNGG AFSAGWNNIG NALFRKGKKF DSTRTHHQLG NISINYNASF 100
NPGGNSYLCV YGWTQSPLAE YYIVDSWGTY RPTGAYKGSF YADGGTYDIY 150
ETTRVNQPSI IGIATFKQYW SVRQTKRTSG TVSVSAHFRK WESLGMPMGK 200
MYETAFTVEG YQSSGSANVM TNQLFIGN 228
Length:228
Mass (Da):25,491
Last modified:February 1, 1996 - v2
Checksum:i32EF9833E7B5E503
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00660 Genomic DNA. Translation: CAA25278.1.
PIRiA00848. WWBSXP.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X00660 Genomic DNA. Translation: CAA25278.1 .
PIRi A00848. WWBSXP.

3D structure databases

ProteinModelPortali P00694.
SMRi P00694. Positions 27-227.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH11. Glycoside Hydrolase Family 11.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00114 .

Family and domain databases

Gene3Di 2.60.120.180. 1 hit.
InterProi IPR008985. ConA-like_lec_gl_sf.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view ]
Pfami PF00457. Glyco_hydro_11. 1 hit.
[Graphical view ]
PRINTSi PR00911. GLHYDRLASE11.
SUPFAMi SSF49899. SSF49899. 1 hit.
PROSITEi PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
PS00777. GLYCOSYL_HYDROL_F11_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The complete nucleotide sequence of the xylanase gene (xynA) of Bacillus pumilus."
    Fukusaki E., Panbangred W., Shinmyo A., Okada H.
    FEBS Lett. 171:197-201(1984)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: IPO.
  2. Urabe I.
    Submitted (FEB-1991) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 103.
  3. "Site-directed mutagenesis at aspartate and glutamate residues of xylanase from Bacillus pumilus."
    Ko E.P., Akatsuka H., Moriyama H., Shinmyo A., Hata Y., Katsube Y., Urabe I., Okada H.
    Biochem. J. 288:117-121(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS, ACTIVE SITES.

Entry informationi

Entry nameiXYNA_BACPU
AccessioniPrimary (citable) accession number: P00694
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: February 1, 1996
Last modified: November 13, 2013
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

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

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