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P26514

- XYNA_STRLI

UniProt

P26514 - XYNA_STRLI

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Protein
Endo-1,4-beta-xylanase A
Gene
xlnA
Organism
Streptomyces lividans
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Contributes to hydrolyze hemicellulose, the major component of plant cell-walls. XLNA and XLNB seem to act sequentially on the substrate to yield xylobiose and xylose as carbon sources.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei169 – 1691Proton donor
Active sitei277 – 2771Nucleophile

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

Keywords - Ligandi

Lectin

Enzyme and pathway databases

BRENDAi3.2.1.8. 6052.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GH10. Glycoside Hydrolase Family 10.

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:xlnA
OrganismiStreptomyces lividans
Taxonomic identifieri1916 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 41411 Publication
Add
BLAST
Chaini42 – 477436Endo-1,4-beta-xylanase A
PRO_0000007979Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi364 ↔ 3831 Publication
Disulfide bondi406 ↔ 4231 Publication
Disulfide bondi447 ↔ 4661 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi46 – 516
Turni52 – 543
Beta strandi56 – 616
Helixi63 – 653
Helixi69 – 7810
Beta strandi80 – 867
Helixi90 – 934
Helixi103 – 11412
Beta strandi118 – 1258
Beta strandi127 – 1293
Helixi132 – 1354
Helixi139 – 15618
Turni157 – 1604
Beta strandi162 – 1687
Beta strandi173 – 1764
Helixi183 – 1864
Helixi191 – 20212
Beta strandi206 – 2149
Helixi221 – 23616
Beta strandi242 – 2454
Beta strandi248 – 2503
Beta strandi251 – 2533
Helixi259 – 2679
Turni268 – 2703
Beta strandi272 – 2809
Helixi285 – 29612
Beta strandi301 – 3077
Helixi311 – 3133
Helixi317 – 3193
Beta strandi322 – 3243
Helixi332 – 34110
Turni359 – 3613
Beta strandi364 – 3663
Helixi368 – 3703
Beta strandi379 – 3813
Helixi387 – 3893
Beta strandi391 – 3933
Beta strandi399 – 4013
Turni402 – 4043
Beta strandi405 – 4106
Beta strandi417 – 4226
Helixi427 – 4293
Beta strandi431 – 4333
Beta strandi439 – 4413
Turni442 – 4443
Beta strandi447 – 4504
Helixi451 – 4533
Beta strandi460 – 4645
Helixi470 – 4723

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E0VX-ray1.70A42-343[»]
1E0WX-ray1.20A42-343[»]
1E0XX-ray1.65A/B42-350[»]
1KNLX-ray1.20A348-477[»]
1KNMX-ray1.20A348-477[»]
1MC9X-ray1.70A348-477[»]
1OD8X-ray1.05A42-354[»]
1V0KX-ray1.03A42-354[»]
1V0LX-ray0.98A42-354[»]
1V0MX-ray1.07A42-354[»]
1V0NX-ray1.10A42-354[»]
1XASX-ray2.60A42-340[»]
ProteinModelPortaliP26514.
SMRiP26514. Positions 42-477.

Miscellaneous databases

EvolutionaryTraceiP26514.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini361 – 477117Ricin B-type lectin
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P26514-1 [UniParc]FASTAAdd to Basket

« Hide

MGSYALPRSG VRRSIRVLLL ALVVGVLGTA TALIAPPGAH AAESTLGAAA    50
AQSGRYFGTA IASGRLSDST YTSIAGREFN MVTAENEMKI DATEPQRGQF 100
NFSSADRVYN WAVQNGKQVR GHTLAWHSQQ PGWMQSLSGS ALRQAMIDHI 150
NGVMAHYKGK IVQWDVVNEA FADGSSGARR DSNLQRSGND WIEVAFRTAR 200
AADPSAKLCY NDYNVENWTW AKTQAMYNMV RDFKQRGVPI DCVGFQSHFN 250
SGSPYNSNFR TTLQNFAALG VDVAITELDI QGAPASTYAN VTNDCLAVSR 300
CLGITVWGVR DSDSWRSEQT PLLFNNDGSK KAAYTAVLDA LNGGDSSEPP 350
ADGGQIKGVG SGRCLDVPDA STSDGTQLQL WDCHSGTNQQ WAATDAGELR 400
VYGDKCLDAA GTSNGSKVQI YSCWGGDNQK WRLNSDGSVV GVQSGLCLDA 450
VGNGTANGTL IQLYTCSNGS NQRWTRT 477
Length:477
Mass (Da):51,163
Last modified:May 30, 2000 - v2
Checksum:iE14A7FE37BDC68CC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64551 Genomic DNA. Translation: AAC26525.1.
PIRiJS0589.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64551 Genomic DNA. Translation: AAC26525.1 .
PIRi JS0589.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E0V X-ray 1.70 A 42-343 [» ]
1E0W X-ray 1.20 A 42-343 [» ]
1E0X X-ray 1.65 A/B 42-350 [» ]
1KNL X-ray 1.20 A 348-477 [» ]
1KNM X-ray 1.20 A 348-477 [» ]
1MC9 X-ray 1.70 A 348-477 [» ]
1OD8 X-ray 1.05 A 42-354 [» ]
1V0K X-ray 1.03 A 42-354 [» ]
1V0L X-ray 0.98 A 42-354 [» ]
1V0M X-ray 1.07 A 42-354 [» ]
1V0N X-ray 1.10 A 42-354 [» ]
1XAS X-ray 2.60 A 42-340 [» ]
ProteinModelPortali P26514.
SMRi P26514. Positions 42-477.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM13. Carbohydrate-Binding Module Family 13.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00114 .
BRENDAi 3.2.1.8. 6052.

Miscellaneous databases

EvolutionaryTracei P26514.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF00331. Glyco_hydro_10. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view ]
PRINTSi PR00134. GLHYDRLASE10.
SMARTi SM00633. Glyco_10. 1 hit.
SM00458. RICIN. 1 hit.
[Graphical view ]
SUPFAMi SSF50370. SSF50370. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEi PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Sequences of three genes specifying xylanases in Streptomyces lividans."
    Shareck F., Roy C., Yaguchi M., Morosoli R., Kluepfel D.
    Gene 107:75-82(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 42-92.
    Strain: 66 / 1326.
  2. Shareck F.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO 20 AND 140-141.
  3. "Crystal structure, at 2.6-A resolution, of the Streptomyces lividans xylanase A, a member of the F family of beta-1,4-D-glycanases."
    Derewenda U., Swenson L., Green R., Wei Y.Y., Morosoli R., Shareck F., Kluepfel D., Derewenda Z.S.
    J. Biol. Chem. 269:20811-20814(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 42-340.
  4. "High-resolution crystal structures of the lectin-like xylan binding domain from Streptomyces lividans xylanase 10A with bound substrates reveal a novel mode of xylan binding."
    Notenboom V., Boraston A.B., Williams S.J., Kilburn D.G., Rose D.R.
    Biochemistry 41:4246-4254(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 348-477, DISULFIDE BONDS.

Entry informationi

Entry nameiXYNA_STRLI
AccessioniPrimary (citable) accession number: P26514
Secondary accession number(s): P96464
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: May 30, 2000
Last modified: July 9, 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

3D-structure, Direct protein sequencing

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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