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Protein

Beta-xylanase

Gene
N/A
Organism
Streptomyces olivaceoviridis (Streptomyces corchorusii)
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei338 – 3381GalactoseCombined sources
Binding sitei343 – 3431GalactoseCombined sources
Binding sitei347 – 3471GalactoseCombined sources
Binding sitei430 – 4301GalactoseCombined sources

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotation, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradationUniRule annotation

Enzyme and pathway databases

BRENDAi3.2.1.8. 6067.

Protein family/group databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-xylanaseUniRule annotation (EC:3.2.1.8UniRule annotation)
OrganismiStreptomyces olivaceoviridis (Streptomyces corchorusii)Imported
Taxonomic identifieri1921 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

Pathology & Biotechi

Chemistry

DrugBankiDB04465. Lactose.

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi168 ↔ 201Combined sources
Disulfide bondi254 ↔ 260Combined sources
Disulfide bondi323 ↔ 342Combined sources
Disulfide bondi365 ↔ 382Combined sources
Disulfide bondi406 ↔ 425Combined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ISVX-ray2.10A/B1-436[»]
1ISWX-ray2.10A/B1-436[»]
1ISXX-ray2.10A/B1-436[»]
1ISYX-ray2.10A/B1-436[»]
1ISZX-ray2.00A/B1-436[»]
1IT0X-ray2.00A/B1-436[»]
1V6UX-ray2.10A/B1-436[»]
1V6VX-ray2.10A/B1-436[»]
1V6WX-ray2.00A/B1-436[»]
1V6XX-ray2.10A/B1-436[»]
1V6YX-ray2.20A218-239[»]
1XYFX-ray1.90A/B1-436[»]
2D1ZX-ray1.60A/B1-436[»]
2D20X-ray1.85A/B1-436[»]
2D22X-ray1.70A/B1-436[»]
2D23X-ray1.95A/B1-436[»]
2D24X-ray1.85A/B1-436[»]
2G3IX-ray2.10A1-303[»]
2G3JX-ray2.70A1-303[»]
2G4FX-ray2.65A/B1-302[»]
ProteinModelPortaliQ7SI98.
SMRiQ7SI98. Positions 1-436.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SI98.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 299299GH10 (glycosyl hydrolase family 10)InterPro annotationAdd
BLAST
Domaini320 – 436117Ricin B-type lectinInterPro annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni325 – 3284Galactose bindingCombined sources
Regioni408 – 4114Galactose bindingCombined sources

Sequence similaritiesi

Belongs to the glycosyl hydrolase 10 (cellulase F) family.UniRule annotation

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.

Q7SI98-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
AESTLGAAAA QSGRYFGTAI ASGKLGDSAY TTIASREFNM VTAENEMKID
60 70 80 90 100
ATEPQRGQFN FSAGDRVYNW AVQNGKQVRG HTLAWHSQQP GWMQSLSGST
110 120 130 140 150
LRQAMIDHIN GVMGHYKGKI AQWDVVNEAF SDDGSGGRRD SNLQRTGNDW
160 170 180 190 200
IEVAFRTARA ADPAAKLCYN DYNIENWTWA KTQGVYNMVR DFKQRGVPID
210 220 230 240 250
CVGFQSHFNS GSPYNSNFRT TLQNFAALGV DVAITELDIQ GASSSTYAAV
260 270 280 290 300
TNDCLAVSRC LGITVWGVRD TDSWRSGDTP LLFNGDGSKK AAYTAVLNAL
310 320 330 340 350
NGGSSTPPPS GGGQIKGVGS GRCLDVPNAS TTDGTQVQLY DCHSATNQQW
360 370 380 390 400
TYTDAGELRV YGDKCLDAAG TGNGTKVQIY SCWGGDNQKW RLNSDGSIVG
410 420 430
VQSGLCLDAV GGGTANGTLI QLYSCSNGSN QRWTRT
Length:436
Mass (Da):46,749
Last modified:December 15, 2003 - v1
Checksum:i6F26B9EC33801083
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ISVX-ray2.10A/B1-436[»]
1ISWX-ray2.10A/B1-436[»]
1ISXX-ray2.10A/B1-436[»]
1ISYX-ray2.10A/B1-436[»]
1ISZX-ray2.00A/B1-436[»]
1IT0X-ray2.00A/B1-436[»]
1V6UX-ray2.10A/B1-436[»]
1V6VX-ray2.10A/B1-436[»]
1V6WX-ray2.00A/B1-436[»]
1V6XX-ray2.10A/B1-436[»]
1V6YX-ray2.20A218-239[»]
1XYFX-ray1.90A/B1-436[»]
2D1ZX-ray1.60A/B1-436[»]
2D20X-ray1.85A/B1-436[»]
2D22X-ray1.70A/B1-436[»]
2D23X-ray1.95A/B1-436[»]
2D24X-ray1.85A/B1-436[»]
2G3IX-ray2.10A1-303[»]
2G3JX-ray2.70A1-303[»]
2G4FX-ray2.65A/B1-302[»]
ProteinModelPortaliQ7SI98.
SMRiQ7SI98. Positions 1-436.
ModBaseiSearch...
MobiDBiSearch...

Chemistry

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

BRENDAi3.2.1.8. 6067.

Miscellaneous databases

EvolutionaryTraceiQ7SI98.

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 nameiQ7SI98_STROI
AccessioniPrimary (citable) accession number: Q7SI98
Secondary accession number(s): Q7SID1
Entry historyi
Integrated into UniProtKB/TrEMBL: December 15, 2003
Last sequence update: December 15, 2003
Last modified: April 13, 2016
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.