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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 PublicationPROSITE-ProRule annotation
Active sitei200 – 2001Proton donor1 PublicationPROSITE-ProRule annotation

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

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 – 2828Add
BLAST
Chaini29 – 213185Endo-1,4-beta-xylanase1 PublicationPRO_0000007996Add
BLAST

Structurei

Secondary structure

1
213
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi33 – 386Combined sources
Beta strandi42 – 487Combined sources
Beta strandi53 – 608Combined sources
Beta strandi62 – 7211Combined sources
Beta strandi78 – 10124Combined sources
Turni102 – 1043Combined sources
Beta strandi105 – 11511Combined sources
Beta strandi121 – 1288Combined sources
Beta strandi131 – 14414Combined sources
Beta strandi148 – 16215Combined sources
Beta strandi166 – 1683Combined sources
Beta strandi170 – 1734Combined sources
Helixi174 – 18310Combined sources
Beta strandi190 – 20314Combined sources
Beta strandi205 – 2139Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09850.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di2.60.120.180. 1 hit.
InterProiIPR013320. ConA-like_dom.
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

        10         20         30         40         50
MFKFKKNFLV GLSAALMSIS LFSATASAAS TDYWQNWTDG GGIVNAVNGS
60 70 80 90 100
GGNYSVNWSN TGNFVVGKGW TTGSPFRTIN YNAGVWAPNG NGYLTLYGWT
110 120 130 140 150
RSPLIEYYVV DSWGTYRPTG TYKGTVKSDG GTYDIYTTTR YNAPSIDGDR
160 170 180 190 200
TTFTQYWSVR QSKRPTGSNA TITFTNHVNA WKSHGMNLGS NWAYQVMATE
210
GYQSSGSSNV TVW
Length:213
Mass (Da):23,359
Last modified:July 1, 1989 - v1
Checksum:i4BA0A35238CC0135
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07723 Genomic DNA. Translation: CAA30553.1.
PIRiS01734.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X07723 Genomic DNA. Translation: CAA30553.1 .
PIRi S01734.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...
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 .
SABIO-RK P09850.

Miscellaneous databases

EvolutionaryTracei P09850.

Family and domain databases

Gene3Di 2.60.120.180. 1 hit.
InterProi IPR013320. ConA-like_dom.
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: November 26, 2014
This is version 94 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