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Q12667

- XYNA_PIRSP

UniProt

Q12667 - XYNA_PIRSP

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Protein
Endo-1,4-beta-xylanase A
Gene
XYNA
Organism
Piromyces sp.
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

Hydrolyzes 1,4-beta linked polysaccharide backbones of xylans, one of the major hemicellulose components in hardwoods and softwoods. It is more active against xylopentaose than xylotetraose, has trace activity against xylotriose. The major products released from hydrolysis of xylooligosaccharides are xylobiose and xylotriose. The reiterated 40 AA domain is involved in binding the cellulase-hemicellulase complex.

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei510 – 5101Nucleophile By similarity
Active sitei603 – 6031Proton donor By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11A_PIRSP.

Names & Taxonomyi

Protein namesi
Recommended name:
Endo-1,4-beta-xylanase A (EC:3.2.1.8)
Alternative name(s):
1,4-beta-D-xylan xylanohydrolase
Xylanase A
Short name:
XYLA
Gene namesi
Name:XYNA
OrganismiPiromyces sp.
Taxonomic identifieri45796 [NCBI]
Taxonomic lineageiEukaryotaFungiNeocallimastigomycotaNeocallimastigomycetesNeocallimastigalesNeocallimastigaceaePiromyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919 Reviewed prediction
Add
BLAST
Chaini20 – 625606Endo-1,4-beta-xylanase A
PRO_0000008017Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ12667.
SMRiQ12667. Positions 292-323.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati259 – 268101
Repeati269 – 278102
Domaini286 – 32338CBM10 1
Add
BLAST
Domaini338 – 37033CBM10 2
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 254235Catalytic 1
Add
BLAST
Regioni255 – 27925Linker
Add
BLAST
Regioni259 – 278202 X 10 AA tandem repeats of G-Q-G-[LQ]-G-N-G-Q-G-[NQ]
Add
BLAST
Regioni374 – 40330Linker
Add
BLAST
Regioni404 – 625222Catalytic 2
Add
BLAST

Domaini

Consists of an N- and C-terminal catalytic domains linked to a middle reiterated domain. Only the C-terminal catalytic domain is active.

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal

Family and domain databases

Gene3Di2.60.120.180. 2 hits.
3.90.1220.10. 2 hits.
InterProiIPR002883. CBM10/Dockerin_dom.
IPR008985. ConA-like_lec_gl_sf.
IPR009034. Dockerin_dom_fun.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view]
PfamiPF02013. CBM_10. 2 hits.
PF00457. Glyco_hydro_11. 2 hits.
[Graphical view]
PRINTSiPR00911. GLHYDRLASE11.
SUPFAMiSSF49899. SSF49899. 2 hits.
SSF64571. SSF64571. 2 hits.
PROSITEiPS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q12667-1 [UniParc]FASTAAdd to Basket

« Hide

MKLFQIFPLL LSLTSVTLAA DDFCNATGFQ GQSVVSTGHD VKKIGNIDYE    50
QWADGGNNSA TFYSDGSFKC NFSNTKDYLC RSGVAFSQAK YPSEIGHIEA 100
EYRLVKKSAS NVGYSYVGVY GWTLQSGISG VYEYYIVDNW LSQWRPGDWV 150
GNTKFGDFTI DGGVYTVYKN VNGNLTQYFS LRKSERTCGT IDVTAHFAQW 200
EKLGLKMPKI TEIKVLAEAG NTGGGCSGSV EIPYAKIYIN GKDQDGKSKG 250
GSSSGGSNGQ GLGNGQGNGQ GQGNGQGQSA TGSGKCPSTI TSQGYKCCSS 300
NCDIIYRDQS GDWGVENDEW CGCGSRVPKT TNCPSSIKNQ GYKCCSDSCE 350
IVLTDSDGDW GIENDEWCGC GIKNTTPTTT TKKSNNSQPT QGQSNNNSST 400
NTNFCSTSKH SGQSVTETSN KVGSIGGVGY ELWADSGNNS ATFYSDGSFS 450
CSFRNAKDYL CRSGLSFDST KTYQQLGHMY ADFKLVKQNI QNVDYSYVGI 500
YGWTRNPLVE FYVVDNWLSQ WRPGDWVGNK KHGDFTIDGA KYTVYENTRT 550
GPSIDGNTTF KQYFSIRQQA RDCGTIDITA HFEQWEKLGM RMGKMHEAKV 600
LGEAGSTGSG TSGTADFPYA KVYIK 625
Length:625
Mass (Da):68,049
Last modified:November 1, 1996 - v1
Checksum:i9DA99B6A17290922
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X91858 mRNA. Translation: CAA62969.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X91858 mRNA. Translation: CAA62969.1 .

3D structure databases

ProteinModelPortali Q12667.
SMRi Q12667. Positions 292-323.
ModBasei Search...

Protein family/group databases

CAZyi GH11. Glycoside Hydrolase Family 11.
mycoCLAPi XYN11A_PIRSP.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00114 .

Family and domain databases

Gene3Di 2.60.120.180. 2 hits.
3.90.1220.10. 2 hits.
InterProi IPR002883. CBM10/Dockerin_dom.
IPR008985. ConA-like_lec_gl_sf.
IPR009034. Dockerin_dom_fun.
IPR001137. Glyco_hydro_11.
IPR013319. Glyco_hydro_11/12.
IPR018208. Glyco_hydro_11_AS.
[Graphical view ]
Pfami PF02013. CBM_10. 2 hits.
PF00457. Glyco_hydro_11. 2 hits.
[Graphical view ]
PRINTSi PR00911. GLHYDRLASE11.
SUPFAMi SSF49899. SSF49899. 2 hits.
SSF64571. SSF64571. 2 hits.
PROSITEi PS00776. GLYCOSYL_HYDROL_F11_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The conserved noncatalytic 40-residue sequence in cellulases and hemicellulases from anaerobic fungi functions as a protein docking domain."
    Fanutti C., Ponyi T., Black G.W., Hazlewood G.P., Gilbert H.J.
    J. Biol. Chem. 270:29314-29322(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiXYNA_PIRSP
AccessioniPrimary (citable) accession number: Q12667
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: September 3, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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