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P07529

- XYNA_CRYAL

UniProt

P07529 - XYNA_CRYAL

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Protein

Endo-1,4-beta-xylanase

Gene
N/A
Organism
Cryptococcus albidus (Filobasidium floriforme)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at protein leveli

Functioni

Requires at least three xylose residues for catalytic activity. Does not have activity against xylobiose.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei120 – 1201Proton donor By similarity
Active sitei214 – 2141Nucleophile By similarity

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_CRYAL.

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
OrganismiCryptococcus albidus (Filobasidium floriforme)
Taxonomic identifieri100951 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaBasidiomycotaAgaricomycotinaTremellomycetesFilobasidialesmitosporic FilobasidialesCryptococcus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 21211 PublicationAdd
BLAST
Chaini22 – 332311Endo-1,4-beta-xylanasePRO_0000007971Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi128 ↔ 160 By similarity
Disulfide bondi247 ↔ 253 By similarity

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliP07529.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.80. 2 hits.
InterProiIPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00331. Glyco_hydro_10. 2 hits.
[Graphical view]
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.

P07529-1 [UniParc]FASTAAdd to Basket

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MLSSTTLLAI LSALALTSVQ AAPADKNSLD YLANKAGKRY LGTAVQSPQL    50
VPGSQYVQIL ESQFDAITPE NEMKWEVVEP TEGNFDFTGT DKIVAEAKKT 100
GSLLRGHNIC WDSQLRYAHE VAPKMKLCIN DYNIETVNAK SQAMAKVAAG 150
LLAKGAPLHC IGMFKNAKRR SSGLLIRTAS SGLESHFIGG STPKDIPAAM 200
NLFSDQGLEV PMTELDVRIP VNGNDMPANA TVAKEQVDDY YTSVSACLGN 250
DLCPGVSIWQ FADPTSWIPG VFKGKLIAVS CTFSGCLLQY CVGYGAALLY 300
DAQYQPKSTY YVVQQALKDG KNSGSKFHGI KL 332
Length:332
Mass (Da):35,776
Last modified:July 1, 1989 - v2
Checksum:i1814FD823E48306A
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti88 – 903TGT → AGL AA sequence 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X12596 Genomic DNA. Translation: CAA31109.1.
PIRiJS0734.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X12596 Genomic DNA. Translation: CAA31109.1 .
PIRi JS0734.

3D structure databases

ProteinModelPortali P07529.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH10. Glycoside Hydrolase Family 10.
mycoCLAPi XYN10A_CRYAL.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 3.20.20.80. 2 hits.
InterProi IPR001000. Glyco_hydro_10.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00331. Glyco_hydro_10. 2 hits.
[Graphical view ]
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. "Complete nucleotide sequence of the xylanase gene from the yeast Cryptococcus albidus."
    Boucher F., Morosoli R., Durand S.
    Nucleic Acids Res. 16:9874-9874(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: CCY 17-4-4.
  2. "Isolation and partial primary sequence of a xylanase from the yeast Cryptococcus albidus."
    Morosoli R., Roy C., Yaguchi M.
    Biochim. Biophys. Acta 870:473-478(1986)
    Cited for: PROTEIN SEQUENCE OF 22-93.

Entry informationi

Entry nameiXYNA_CRYAL
AccessioniPrimary (citable) accession number: P07529
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: July 1, 1989
Last modified: November 13, 2013
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3