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Protein

Endo-1,4-beta-xylanase A

Gene

xlnA

Organism
Streptomyces lividans
Status
Reviewed-Annotation score: 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: xylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei169Proton donor1
Active sitei277Nucleophile1

GO - Molecular functioni

GO - Biological processi

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 lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Chemistry databases

DrugBankiDB04465. Lactose.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 411 PublicationAdd BLAST41
ChainiPRO_000000797942 – 477Endo-1,4-beta-xylanase AAdd BLAST436

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi364 ↔ 383PROSITE-ProRule annotation1 Publication
Disulfide bondi406 ↔ 423PROSITE-ProRule annotation1 Publication
Disulfide bondi447 ↔ 466PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1477
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi46 – 51Combined sources6
Turni52 – 54Combined sources3
Beta strandi56 – 61Combined sources6
Helixi63 – 65Combined sources3
Helixi69 – 78Combined sources10
Beta strandi80 – 86Combined sources7
Helixi90 – 93Combined sources4
Helixi103 – 114Combined sources12
Beta strandi118 – 125Combined sources8
Beta strandi127 – 129Combined sources3
Helixi132 – 135Combined sources4
Helixi139 – 156Combined sources18
Turni157 – 160Combined sources4
Beta strandi162 – 168Combined sources7
Beta strandi173 – 176Combined sources4
Helixi183 – 186Combined sources4
Helixi191 – 202Combined sources12
Beta strandi206 – 214Combined sources9
Helixi221 – 236Combined sources16
Beta strandi242 – 245Combined sources4
Beta strandi248 – 250Combined sources3
Beta strandi251 – 253Combined sources3
Helixi259 – 267Combined sources9
Turni268 – 270Combined sources3
Beta strandi272 – 280Combined sources9
Helixi285 – 296Combined sources12
Beta strandi301 – 307Combined sources7
Helixi311 – 313Combined sources3
Helixi317 – 319Combined sources3
Beta strandi322 – 324Combined sources3
Helixi332 – 341Combined sources10
Turni359 – 361Combined sources3
Beta strandi364 – 366Combined sources3
Helixi368 – 370Combined sources3
Beta strandi379 – 381Combined sources3
Helixi387 – 389Combined sources3
Beta strandi391 – 393Combined sources3
Beta strandi399 – 401Combined sources3
Turni402 – 404Combined sources3
Beta strandi405 – 410Combined sources6
Beta strandi417 – 422Combined sources6
Helixi427 – 429Combined sources3
Beta strandi431 – 433Combined sources3
Beta strandi439 – 441Combined sources3
Turni442 – 444Combined sources3
Beta strandi447 – 450Combined sources4
Helixi451 – 453Combined sources3
Beta strandi460 – 464Combined sources5
Helixi470 – 472Combined sources3

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP26514.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini42 – 340GH10PROSITE-ProRule annotationAdd BLAST299
Domaini361 – 477Ricin B-type lectinPROSITE-ProRule annotationAdd BLAST117

Sequence similaritiesi

Contains 1 GH10 (glycosyl hydrolase family 10) domain.PROSITE-ProRule annotation
Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. GH10.
IPR031158. GH10_AS.
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. GH10_1. 1 hit.
PS51760. GH10_2. 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.
PIRiJS0589.

3D structure databases

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

Chemistry databases

DrugBankiDB04465. Lactose.

Protein family/group databases

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

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.
BRENDAi3.2.1.8. 6052.

Miscellaneous databases

EvolutionaryTraceiP26514.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. GH10.
IPR031158. GH10_AS.
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. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 2, 2016
This is version 111 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.