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Protein

Beta-xylanase

Gene

xysA

Organism
Streptomyces halstedii
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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

GlycosidaseUniRule annotationImported, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradationUniRule annotation

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH10. Glycoside Hydrolase Family 10.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-xylanaseUniRule annotation (EC:3.2.1.8UniRule annotation)
Gene namesi
Name:xysAImported
OrganismiStreptomyces halstediiImported
Taxonomic identifieri1944 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 4545Sequence analysisAdd
BLAST
Chaini46 – 461416Beta-xylanaseSequence analysisPRO_5004252501Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi213 ↔ 245Combined sources
Disulfide bondi301 ↔ 307Combined sources

Keywords - PTMi

Disulfide bondUniRule annotation

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NQ6X-ray1.78A46-347[»]
ProteinModelPortaliQ59922.
SMRiQ59922. Positions 58-347.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ59922.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 346304GH10 (glycosyl hydrolase family 10)InterPro annotationAdd
BLAST
Domaini358 – 461104CBM2 (carbohydrate binding type-2)InterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 10 (cellulase F) family.UniRule annotation
Contains 1 CBM2 (carbohydrate binding type-2) domain.UniRule annotation

Keywords - Domaini

SignalSequence analysis

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001000. GH10.
IPR031158. GH10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00637. CBD_II. 1 hit.
SM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00591. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q59922-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQNPPVGGR TRRRPQARAR CALSLLTAGV LAAAGVVALA GTAQAAGALG
60 70 80 90 100
DAAAAKGRYF GAAVAANHLG EAAYASTLDA QFGSVTPENE MKWDAVESSR
110 120 130 140 150
NSFSFSAADR IVSHAQSKGM KVRGHTLVWH SQLPGWVSPL AATDLRSAMN
160 170 180 190 200
NHITQVMTHY KGKIHSWDVV NEAFQDGGSG ARRSSPFQDK LGNGFIEEAF
210 220 230 240 250
RTARTVDADA KLCYNDYNTD GQNAKSNAVY EMVKDFKQRG VPIDCVGFQS
260 270 280 290 300
HFNSNSPVPS DFQANLQRFA DLGVDVQITE LDIEGSGSAQ AANYTKVVNA
310 320 330 340 350
CLAVTRCTGI TVWGVTDKYS WRSGGTPLLF DGDYNKKPAY DAVLAALGGS
360 370 380 390 400
GGGGDDGGEG GDGACTATYT RTSTWNGGYN GQVTVKAGGS GITGWAVPVT
410 420 430 440 450
VASPQKVSAV WNGTPTTTGD VMTVRHSWNG TLAAGASTTF GFTVQTNGGT
460
SAPVVGACTA S
Length:461
Mass (Da):47,930
Last modified:November 1, 1996 - v1
Checksum:i086A7EE6B7C78341
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41627 Genomic DNA. Translation: AAC45554.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41627 Genomic DNA. Translation: AAC45554.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NQ6X-ray1.78A46-347[»]
ProteinModelPortaliQ59922.
SMRiQ59922. Positions 58-347.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM2. Carbohydrate-Binding Module Family 2.
GH10. Glycoside Hydrolase Family 10.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiQ59922.

Family and domain databases

Gene3Di2.60.40.290. 1 hit.
3.20.20.80. 1 hit.
InterProiIPR008965. Carb-bd_dom.
IPR001919. CBD2.
IPR012291. CBD_carb-bd_dom.
IPR018366. CBM2_CS.
IPR001000. GH10.
IPR031158. GH10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00553. CBM_2. 1 hit.
PF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00637. CBD_II. 1 hit.
SM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF49384. SSF49384. 1 hit.
SSF51445. SSF51445. 1 hit.
PROSITEiPS51173. CBM2. 1 hit.
PS00561. CBM2_A. 1 hit.
PS00591. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Analysis of xysA, a gene from Streptomyces halstedii JM8 that encodes a 45-kilodalton modular xylanase, Xys1."
    Ruiz-Arribas A., Sanchez P., Calvete J.J., Raida M., Fernandez-Abalos J.M., Santamaria R.I.
    Appl. Environ. Microbiol. 63:2983-2988(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: JM8Imported.
  2. Cited for: X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 46-347, DISULFIDE BONDS.

Entry informationi

Entry nameiQ59922_STRHA
AccessioniPrimary (citable) accession number: Q59922
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: April 13, 2016
This is version 86 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.