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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)DescriptionActionsGraphical viewLength
Active sitei236NucleophilePROSITE-ProRule annotation1
Binding sitei338GalactoseCombined sources1
Binding sitei343GalactoseCombined sources1
Binding sitei347GalactoseCombined sources1
Binding sitei430GalactoseCombined sources1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidaseUniRule annotation, Hydrolase
Biological processCarbohydrate 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 databases

DrugBankiDB03389. alpha-D-Xylopyranose.
DB02379. Beta-D-Glucose.
DB04465. Lactose.

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
PDB 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-ray2.20A1-300[»]
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ7SI98.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 299GH10InterPro annotationAdd BLAST299
Domaini320 – 436Ricin B-type lectinInterPro annotationAdd BLAST117

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni325 – 328Galactose bindingCombined sources4
Regioni408 – 411Galactose bindingCombined sources4

Sequence similaritiesi

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

Family and domain databases

InterProiView protein in InterPro
IPR001000. GH10.
IPR031158. GH10_AS.
IPR017853. Glycoside_hydrolase_SF.
IPR000772. Ricin_B_lectin.
PfamiView protein in Pfam
PF00331. Glyco_hydro_10. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
PRINTSiPR00134. GLHYDRLASE10.
SMARTiView protein in SMART
SM00633. Glyco_10. 1 hit.
SM00458. RICIN. 1 hit.
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiView protein in PROSITE
PS00591. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
PS50231. RICIN_B_LECTIN. 1 hit.

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

Similar proteinsi

Entry informationi

Entry nameiQ7SI98_STROI
AccessioniPrimary (citable) accession number: Q7SI98
Secondary accession number(s): Q7SID1
Entry historyiIntegrated into UniProtKB/TrEMBL: December 15, 2003
Last sequence update: December 15, 2003
Last modified: September 27, 2017
This is version 90 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources