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P09850

- XYNA_BACCI

UniProt

P09850 - XYNA_BACCI

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Protein
Endo-1,4-beta-xylanase
Gene
xlnA
Organism
Bacillus circulans
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 sitei106 – 1061Nucleophile1 Publication
Active sitei200 – 2001Proton donor1 Publication

GO - Molecular functioni

  1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC
Complete GO annotation...

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

SABIO-RKP09850.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase (EC:3.2.1.8)
Short name:
Xylanase
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase
Gene namesi
Name:xlnA
OrganismiBacillus circulans
Taxonomic identifieri1397 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828
Add
BLAST
Chaini29 – 213185Endo-1,4-beta-xylanase1 Publication
PRO_0000007996Add
BLAST

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 386
Beta strandi42 – 487
Beta strandi53 – 608
Beta strandi62 – 7211
Beta strandi78 – 10124
Turni102 – 1043
Beta strandi105 – 11511
Beta strandi121 – 1288
Beta strandi131 – 14414
Beta strandi148 – 16215
Beta strandi166 – 1683
Beta strandi170 – 1734
Helixi174 – 18310
Beta strandi190 – 20314
Beta strandi205 – 2139

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BCXX-ray1.81A29-213[»]
1BVVX-ray1.80A29-213[»]
1C5HX-ray1.55A29-213[»]
1C5IX-ray1.80A29-213[»]
1HV0X-ray1.60A29-213[»]
1HV1X-ray1.80A29-213[»]
1XNBX-ray1.49A29-213[»]
1XNCX-ray1.60A29-213[»]
2BVVX-ray1.50A29-213[»]
3LB9X-ray3.00A/B/C29-213[»]
3VZJX-ray2.41A/B/C/D29-213[»]
3VZKX-ray1.55A/B29-213[»]
3VZLX-ray2.00A/B/C/D29-213[»]
3VZMX-ray1.86A29-213[»]
3VZNX-ray1.67A/B29-213[»]
3VZOX-ray1.73A29-213[»]
ProteinModelPortaliP09850.
SMRiP09850. Positions 29-213.

Miscellaneous databases

EvolutionaryTraceiP09850.

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.

P09850-1 [UniParc]FASTAAdd to Basket

« Hide

MFKFKKNFLV GLSAALMSIS LFSATASAAS TDYWQNWTDG GGIVNAVNGS    50
GGNYSVNWSN TGNFVVGKGW TTGSPFRTIN YNAGVWAPNG NGYLTLYGWT 100
RSPLIEYYVV DSWGTYRPTG TYKGTVKSDG GTYDIYTTTR YNAPSIDGDR 150
TTFTQYWSVR QSKRPTGSNA TITFTNHVNA WKSHGMNLGS NWAYQVMATE 200
GYQSSGSSNV TVW 213
Length:213
Mass (Da):23,359
Last modified:July 1, 1989 - v1
Checksum:i4BA0A35238CC0135
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07723 Genomic DNA. Translation: CAA30553.1.
PIRiS01734.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X07723 Genomic DNA. Translation: CAA30553.1 .
PIRi S01734.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1BCX X-ray 1.81 A 29-213 [» ]
1BVV X-ray 1.80 A 29-213 [» ]
1C5H X-ray 1.55 A 29-213 [» ]
1C5I X-ray 1.80 A 29-213 [» ]
1HV0 X-ray 1.60 A 29-213 [» ]
1HV1 X-ray 1.80 A 29-213 [» ]
1XNB X-ray 1.49 A 29-213 [» ]
1XNC X-ray 1.60 A 29-213 [» ]
2BVV X-ray 1.50 A 29-213 [» ]
3LB9 X-ray 3.00 A/B/C 29-213 [» ]
3VZJ X-ray 2.41 A/B/C/D 29-213 [» ]
3VZK X-ray 1.55 A/B 29-213 [» ]
3VZL X-ray 2.00 A/B/C/D 29-213 [» ]
3VZM X-ray 1.86 A 29-213 [» ]
3VZN X-ray 1.67 A/B 29-213 [» ]
3VZO X-ray 1.73 A 29-213 [» ]
ProteinModelPortali P09850.
SMRi P09850. Positions 29-213.
ModBasei 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 .
SABIO-RK P09850.

Miscellaneous databases

EvolutionaryTracei P09850.

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. "Nucleotide sequence of a Bacillus circulans xylanase gene."
    Yang R.C.A., MacKenzie C.R., Narang S.A.
    Nucleic Acids Res. 16:7187-7187(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Mutational and crystallographic analyses of the active site residues of the Bacillus circulans xylanase."
    Wakarchuk W.W., Campbell R.L., Sung W.L., Davoodi J., Yaguchi M.
    Protein Sci. 3:467-475(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), MUTAGENESIS.
  3. "The pKa of the general acid/base carboxyl group of a glycosidase cycles during catalysis: a 13C-NMR study of Bacillus circulans xylanase."
    McIntosh L.P., Hand G., Johnson P.E., Joshi M.D., Koerner M., Plesniak L.A., Ziser L., Wakarchuk W.W., Withers S.G.
    Biochemistry 35:9958-9966(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR.

Entry informationi

Entry nameiXYNA_BACCI
AccessioniPrimary (citable) accession number: P09850
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 91 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

3D-structure

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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