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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)DescriptionActionsGraphical viewLength
Active sitei157Proton donor1
Active sitei263Nucleophile1

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)DescriptionActionsGraphical viewLength
Signal peptidei1 – 263 PublicationsAdd BLAST26
ChainiPRO_000000798527 – 329Endo-1,4-beta-xylanaseAdd BLAST303

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei27Pyrrolidone carboxylic acid1
Disulfide bondi281 ↔ 287

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Structurei

Secondary structure

1329
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi27 – 29Combined sources3
Helixi32 – 37Combined sources6
Turni38 – 40Combined sources3
Beta strandi42 – 48Combined sources7
Helixi50 – 53Combined sources4
Helixi58 – 65Combined sources8
Beta strandi67 – 73Combined sources7
Helixi77 – 80Combined sources4
Helixi90 – 102Combined sources13
Beta strandi105 – 112Combined sources8
Beta strandi114 – 116Combined sources3
Helixi119 – 122Combined sources4
Helixi127 – 144Combined sources18
Turni145 – 147Combined sources3
Beta strandi150 – 157Combined sources8
Beta strandi163 – 165Combined sources3
Helixi169 – 173Combined sources5
Helixi178 – 189Combined sources12
Beta strandi193 – 201Combined sources9
Beta strandi205 – 207Combined sources3
Helixi208 – 222Combined sources15
Beta strandi229 – 232Combined sources4
Turni238 – 240Combined sources3
Helixi241 – 252Combined sources12
Beta strandi257 – 266Combined sources10
Helixi271 – 283Combined sources13
Beta strandi287 – 293Combined sources7
Helixi297 – 299Combined sources3
Helixi303 – 305Combined sources3
Beta strandi308 – 310Combined sources3
Helixi318 – 327Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23360.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini29 – 326GH10PROSITE-ProRule annotationAdd BLAST298

Sequence similaritiesi

Contains 1 GH10 (glycosyl hydrolase family 10) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR001000. GH10.
IPR031158. GH10_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. GH10_1. 1 hit.
PS51760. GH10_2. 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)DescriptionActionsGraphical viewLength
Sequence conflicti243G → S in CAB65468 (Ref. 1) Curated1
Sequence conflicti243G → S in AAF24127 (Ref. 1) Curated1
Sequence conflicti271P → S in CAB65468 (Ref. 1) Curated1
Sequence conflicti271P → S in AAF24127 (Ref. 1) Curated1

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
PDB 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.
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. GH10.
IPR031158. GH10_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. GH10_1. 1 hit.
PS51760. GH10_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 2, 2016
This is version 103 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

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.