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Protein

Endo-1,4-beta-xylanase

Gene

XYNA

Organism
Thermoascus aurantiacus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei157 – 1571Proton donor
Active sitei263 – 2631Nucleophile

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Protein family/group databases

CAZyiGH10. Glycoside Hydrolase Family 10.
mycoCLAPiXYN10A_THEAU.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase (EC:3.2.1.8)
Short name:
Xylanase
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase
TAXI
Gene namesi
Name:XYNA
OrganismiThermoascus aurantiacus
Taxonomic identifieri5087 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesThermoascaceaeThermoascus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26263 PublicationsAdd
BLAST
Chaini27 – 329303Endo-1,4-beta-xylanasePRO_0000007985Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271Pyrrolidone carboxylic acid
Disulfide bondi281 ↔ 287

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Structurei

Secondary structure

1
329
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi27 – 293Combined sources
Helixi32 – 376Combined sources
Turni38 – 403Combined sources
Beta strandi42 – 487Combined sources
Helixi50 – 534Combined sources
Helixi58 – 658Combined sources
Beta strandi67 – 737Combined sources
Helixi77 – 804Combined sources
Helixi90 – 10213Combined sources
Beta strandi105 – 1128Combined sources
Beta strandi114 – 1163Combined sources
Helixi119 – 1224Combined sources
Helixi127 – 14418Combined sources
Turni145 – 1473Combined sources
Beta strandi150 – 1578Combined sources
Beta strandi163 – 1653Combined sources
Helixi169 – 1735Combined sources
Helixi178 – 18912Combined sources
Beta strandi193 – 2019Combined sources
Beta strandi205 – 2073Combined sources
Helixi208 – 22215Combined sources
Beta strandi229 – 2324Combined sources
Turni238 – 2403Combined sources
Helixi241 – 25212Combined sources
Beta strandi257 – 26610Combined sources
Helixi271 – 28313Combined sources
Beta strandi287 – 2937Combined sources
Helixi297 – 2993Combined sources
Helixi303 – 3053Combined sources
Beta strandi308 – 3103Combined sources
Helixi318 – 32710Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GOKX-ray1.14A28-329[»]
1GOMX-ray1.92A28-329[»]
1GOOX-ray1.87A28-329[»]
1GOQX-ray1.80A28-329[»]
1GORX-ray1.70A28-329[»]
1I1WX-ray0.89A28-329[»]
1I1XX-ray1.11A27-329[»]
1K6AX-ray1.14A27-329[»]
1TUXX-ray1.80A28-325[»]
2BNJX-ray1.60A28-329[»]
3NYDX-ray1.23A/B27-329[»]
3O2LX-ray2.00A27-329[»]
4BS0X-ray1.09A/B28-329[»]
ProteinModelPortaliP23360.
SMRiP23360. Positions 27-328.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23360.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. Glyco_hydro_10.
IPR031158. Glyco_hydro_10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P23360-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVRPTILLTS LLLAPFAAAS PILEERQAAQ SVDQLIKARG KVYFGVATDQ
60 70 80 90 100
NRLTTGKNAA IIQADFGQVT PENSMKWDAT EPSQGNFNFA GADYLVNWAQ
110 120 130 140 150
QNGKLIRGHT LVWHSQLPSW VSSITDKNTL TNVMKNHITT LMTRYKGKIR
160 170 180 190 200
AWDVVNEAFN EDGSLRQTVF LNVIGEDYIP IAFQTARAAD PNAKLYINDY
210 220 230 240 250
NLDSASYPKT QAIVNRVKQW RAAGVPIDGI GSQTHLSAGQ GAGVLQALPL
260 270 280 290 300
LASAGTPEVA ITELDVAGAS PTDYVNVVNA CLNVQSCVGI TVWGVADPDS
310 320
WRASTTPLLF DGNFNPKPAY NAIVQDLQQ
Length:329
Mass (Da):35,686
Last modified:April 27, 2001 - v4
Checksum:i8FE2F3D1A9F89815
GO

Sequence cautioni

The sequence described in Ref. 2 differs from that shown.Sequencing errors.Curated
The sequence described in PubMed:1924265 differs from that shown.Sequencing errors.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti243 – 2431G → S in CAB65468 (Ref. 1) Curated
Sequence conflicti243 – 2431G → S in AAF24127 (Ref. 1) Curated
Sequence conflicti271 – 2711P → S in CAB65468 (Ref. 1) Curated
Sequence conflicti271 – 2711P → S in AAF24127 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132635 Genomic DNA. Translation: CAB65468.1.
AF127529 Genomic DNA. Translation: AAF24127.1.
PIRiA59381.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132635 Genomic DNA. Translation: CAB65468.1.
AF127529 Genomic DNA. Translation: AAF24127.1.
PIRiA59381.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GOKX-ray1.14A28-329[»]
1GOMX-ray1.92A28-329[»]
1GOOX-ray1.87A28-329[»]
1GOQX-ray1.80A28-329[»]
1GORX-ray1.70A28-329[»]
1I1WX-ray0.89A28-329[»]
1I1XX-ray1.11A27-329[»]
1K6AX-ray1.14A27-329[»]
1TUXX-ray1.80A28-325[»]
2BNJX-ray1.60A28-329[»]
3NYDX-ray1.23A/B27-329[»]
3O2LX-ray2.00A27-329[»]
4BS0X-ray1.09A/B28-329[»]
ProteinModelPortaliP23360.
SMRiP23360. Positions 27-328.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH10. Glycoside Hydrolase Family 10.
mycoCLAPiXYN10A_THEAU.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP23360.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. Glyco_hydro_10.
IPR031158. Glyco_hydro_10_AS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 1 hit.
[Graphical view]
PRINTSiPR00134. GLHYDRLASE10.
SMARTiSM00633. Glyco_10. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
PROSITEiPS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cloning, sequencing and overexpression of Thermoascus aurantiacus xylanase A (xynA)."
    Bousson J.-C., Parriche M.
    Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Significance of structural homology of Thermoascus aurantiacus xylanase with the exoglucanase of Cellulomonas fimi."
    Srinivasa B.R., Vithayathil P.J., Roy R.P., Swaminathan K.R.
    J. Protein Chem. 9:337-338(1990)
    Cited for: PROTEIN SEQUENCE OF 27-328.
  3. "The primary structure of xylanase from Thermoascus aurantiacus."
    Srinivasa B.R., Swaminathan K.R., Ganapathy C., Roy R.P., Murthy S.K., Vithayathil P.J.
    Protein Seq. Data Anal. 4:15-20(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-328.
  4. "Anisotropic refinement of the structure of Thermoascus aurantiacus xylanase I."
    Teixeira S., Lo Leggio L., Pickersgill R.W., Cardin C.
    Acta Crystallogr. D 57:385-392(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 27-328, X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS).
    Strain: IMI 216529.
  5. "High resolution structure and sequence of T. aurantiacus xylanase I: implications for the evolution of thermostability in family 10 xylanases and enzymes with (beta)alpha-barrel architecture."
    Lo Leggio L., Kalogiannis S., Bhat M.K., Pickersgill R.W.
    Proteins 36:295-306(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.14 ANGSTROMS).
    Strain: IMI 216529.

Entry informationi

Entry nameiXYNA_THEAU
AccessioniPrimary (citable) accession number: P23360
Secondary accession number(s): Q9UQZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: April 27, 2001
Last modified: June 24, 2015
This is version 97 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

Ref. 2, PubMed:1924265 and PubMed:10409823 N-terminal modification was incorrect. X-ray structure has cyclic pyroglutamic acid.Curated

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.