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Protein

Endo-1,4-beta-xylanase

Gene

XYNA

Organism
Thermoascus aurantiacus
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Caution

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

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

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate 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 acidBy similarity1
Disulfide bondi281 ↔ 287

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Proteomic databases

PRIDEiP23360

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

Keywords - Domaini

Signal

Family and domain databases

InterProiView protein in InterPro
IPR001000 GH10
IPR031158 GH10_AS
IPR017853 Glycoside_hydrolase_SF
PfamiView protein in Pfam
PF00331 Glyco_hydro_10, 1 hit
PRINTSiPR00134 GLHYDRLASE10
SMARTiView protein in SMART
SM00633 Glyco_10, 1 hit
SUPFAMiSSF51445 SSF51445, 1 hit
PROSITEiView protein in PROSITE
PS00591 GH10_1, 1 hit
PS51760 GH10_2, 1 hit

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

Similar proteinsi

Entry informationi

Entry nameiXYNA_THEAU
AccessioniPrimary (citable) accession number: P23360
Secondary accession number(s): Q9UQZ4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: April 27, 2001
Last modified: May 23, 2018
This is version 107 of the entry and version 4 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing
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Main funding by: National Institutes of Health