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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. carbohydrate binding Source: UniProtKB-KW
  2. 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-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 41411 PublicationAdd
BLAST
Chaini42 – 477436Endo-1,4-beta-xylanase APRO_0000007979Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi364 ↔ 3831 PublicationPROSITE-ProRule annotation
Disulfide bondi406 ↔ 4231 PublicationPROSITE-ProRule annotation
Disulfide bondi447 ↔ 4661 PublicationPROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
477
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi46 – 516Combined sources
Turni52 – 543Combined sources
Beta strandi56 – 616Combined sources
Helixi63 – 653Combined sources
Helixi69 – 7810Combined sources
Beta strandi80 – 867Combined sources
Helixi90 – 934Combined sources
Helixi103 – 11412Combined sources
Beta strandi118 – 1258Combined sources
Beta strandi127 – 1293Combined sources
Helixi132 – 1354Combined sources
Helixi139 – 15618Combined sources
Turni157 – 1604Combined sources
Beta strandi162 – 1687Combined sources
Beta strandi173 – 1764Combined sources
Helixi183 – 1864Combined sources
Helixi191 – 20212Combined sources
Beta strandi206 – 2149Combined sources
Helixi221 – 23616Combined sources
Beta strandi242 – 2454Combined sources
Beta strandi248 – 2503Combined sources
Beta strandi251 – 2533Combined sources
Helixi259 – 2679Combined sources
Turni268 – 2703Combined sources
Beta strandi272 – 2809Combined sources
Helixi285 – 29612Combined sources
Beta strandi301 – 3077Combined sources
Helixi311 – 3133Combined sources
Helixi317 – 3193Combined sources
Beta strandi322 – 3243Combined sources
Helixi332 – 34110Combined sources
Turni359 – 3613Combined sources
Beta strandi364 – 3663Combined sources
Helixi368 – 3703Combined sources
Beta strandi379 – 3813Combined sources
Helixi387 – 3893Combined sources
Beta strandi391 – 3933Combined sources
Beta strandi399 – 4013Combined sources
Turni402 – 4043Combined sources
Beta strandi405 – 4106Combined sources
Beta strandi417 – 4226Combined sources
Helixi427 – 4293Combined sources
Beta strandi431 – 4333Combined sources
Beta strandi439 – 4413Combined sources
Turni442 – 4443Combined sources
Beta strandi447 – 4504Combined sources
Helixi451 – 4533Combined sources
Beta strandi460 – 4645Combined sources
Helixi470 – 4723Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP26514.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini361 – 477117Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

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

        10         20         30         40         50
MGSYALPRSG VRRSIRVLLL ALVVGVLGTA TALIAPPGAH AAESTLGAAA
60 70 80 90 100
AQSGRYFGTA IASGRLSDST YTSIAGREFN MVTAENEMKI DATEPQRGQF
110 120 130 140 150
NFSSADRVYN WAVQNGKQVR GHTLAWHSQQ PGWMQSLSGS ALRQAMIDHI
160 170 180 190 200
NGVMAHYKGK IVQWDVVNEA FADGSSGARR DSNLQRSGND WIEVAFRTAR
210 220 230 240 250
AADPSAKLCY NDYNVENWTW AKTQAMYNMV RDFKQRGVPI DCVGFQSHFN
260 270 280 290 300
SGSPYNSNFR TTLQNFAALG VDVAITELDI QGAPASTYAN VTNDCLAVSR
310 320 330 340 350
CLGITVWGVR DSDSWRSEQT PLLFNNDGSK KAAYTAVLDA LNGGDSSEPP
360 370 380 390 400
ADGGQIKGVG SGRCLDVPDA STSDGTQLQL WDCHSGTNQQ WAATDAGELR
410 420 430 440 450
VYGDKCLDAA GTSNGSKVQI YSCWGGDNQK WRLNSDGSVV GVQSGLCLDA
460 470
VGNGTANGTL IQLYTCSNGS NQRWTRT
Length:477
Mass (Da):51,163
Last modified:May 30, 2000 - v2
Checksum:iE14A7FE37BDC68CC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64551 Genomic DNA. Translation: AAC26525.1.
PIRiJS0589.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64551 Genomic DNA. Translation: AAC26525.1 .
PIRi JS0589.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 102 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