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P23360

- XYNA_THEAU

UniProt

P23360 - XYNA_THEAU

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Protein
Endo-1,4-beta-xylanase
Gene
XYNA
Organism
Thermoascus aurantiacus
Status
Reviewed - 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

  1. endo-1,4-beta-xylanase activity Source: UniProtKB-EC

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-KW
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 Publications
Add
BLAST
Chaini27 – 329303Endo-1,4-beta-xylanase
PRO_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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

Miscellaneous databases

EvolutionaryTraceiP23360.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. Glyco_hydro_10.
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

MVRPTILLTS LLLAPFAAAS PILEERQAAQ SVDQLIKARG KVYFGVATDQ    50
NRLTTGKNAA IIQADFGQVT PENSMKWDAT EPSQGNFNFA GADYLVNWAQ 100
QNGKLIRGHT LVWHSQLPSW VSSITDKNTL TNVMKNHITT LMTRYKGKIR 150
AWDVVNEAFN EDGSLRQTVF LNVIGEDYIP IAFQTARAAD PNAKLYINDY 200
NLDSASYPKT QAIVNRVKQW RAAGVPIDGI GSQTHLSAGQ GAGVLQALPL 250
LASAGTPEVA ITELDVAGAS PTDYVNVVNA CLNVQSCVGI TVWGVADPDS 300
WRASTTPLLF DGNFNPKPAY NAIVQDLQQ 329
Length:329
Mass (Da):35,686
Last modified:April 27, 2001 - v4
Checksum:i8FE2F3D1A9F89815
GO

Sequence cautioni

The sequence described in 1 Publication differs from that shown. Reason: Sequencing errors.
The sequence described in 1 Publication differs from that shown. Reason: Sequencing errors.

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ132635 Genomic DNA. Translation: CAB65468.1.
AF127529 Genomic DNA. Translation: AAF24127.1.
PIRiA59381.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ132635 Genomic DNA. Translation: CAB65468.1 .
AF127529 Genomic DNA. Translation: AAF24127.1 .
PIRi A59381.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1GOK X-ray 1.14 A 28-329 [» ]
1GOM X-ray 1.92 A 28-329 [» ]
1GOO X-ray 1.87 A 28-329 [» ]
1GOQ X-ray 1.80 A 28-329 [» ]
1GOR X-ray 1.70 A 28-329 [» ]
1I1W X-ray 0.89 A 28-329 [» ]
1I1X X-ray 1.11 A 27-329 [» ]
1K6A X-ray 1.14 A 27-329 [» ]
1TUX X-ray 1.80 A 28-325 [» ]
2BNJ X-ray 1.60 A 28-329 [» ]
3NYD X-ray 1.23 A/B 27-329 [» ]
3O2L X-ray 2.00 A 27-329 [» ]
4BS0 X-ray 1.09 A/B 28-329 [» ]
ProteinModelPortali P23360.
SMRi P23360. Positions 27-328.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH10. Glycoside Hydrolase Family 10.
mycoCLAPi XYN10A_THEAU.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P23360.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00331. Glyco_hydro_10. 1 hit.
[Graphical view ]
PRINTSi PR00134. GLHYDRLASE10.
SMARTi SM00633. Glyco_10. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
PROSITEi PS00591. GLYCOSYL_HYDROL_F10. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: July 9, 2014
This is version 94 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

1 Publication, 1 Publication and 1 Publication N-terminal modification was incorrect. X-ray structure has cyclic pyroglutamic acid.

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

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