Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q12667

- XYNA_PIRSP

UniProt

Q12667 - XYNA_PIRSP

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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 – 5101NucleophilePROSITE-ProRule annotation
Active sitei603 – 6031Proton donorBy similarity

GO - Molecular functioni

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

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 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 625606Endo-1,4-beta-xylanase APRO_0000008017Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ12667.
SMRiQ12667. Positions 292-323.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 254235Catalytic 1Add
BLAST
Regioni255 – 27925LinkerAdd
BLAST
Regioni259 – 278202 X 10 AA tandem repeats of G-Q-G-[LQ]-G-N-G-Q-G-[NQ]Add
BLAST
Regioni374 – 40330LinkerAdd
BLAST
Regioni404 – 625222Catalytic 2Add
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.
IPR013320. ConA-like_dom.
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

        10         20         30         40         50
MKLFQIFPLL LSLTSVTLAA DDFCNATGFQ GQSVVSTGHD VKKIGNIDYE
60 70 80 90 100
QWADGGNNSA TFYSDGSFKC NFSNTKDYLC RSGVAFSQAK YPSEIGHIEA
110 120 130 140 150
EYRLVKKSAS NVGYSYVGVY GWTLQSGISG VYEYYIVDNW LSQWRPGDWV
160 170 180 190 200
GNTKFGDFTI DGGVYTVYKN VNGNLTQYFS LRKSERTCGT IDVTAHFAQW
210 220 230 240 250
EKLGLKMPKI TEIKVLAEAG NTGGGCSGSV EIPYAKIYIN GKDQDGKSKG
260 270 280 290 300
GSSSGGSNGQ GLGNGQGNGQ GQGNGQGQSA TGSGKCPSTI TSQGYKCCSS
310 320 330 340 350
NCDIIYRDQS GDWGVENDEW CGCGSRVPKT TNCPSSIKNQ GYKCCSDSCE
360 370 380 390 400
IVLTDSDGDW GIENDEWCGC GIKNTTPTTT TKKSNNSQPT QGQSNNNSST
410 420 430 440 450
NTNFCSTSKH SGQSVTETSN KVGSIGGVGY ELWADSGNNS ATFYSDGSFS
460 470 480 490 500
CSFRNAKDYL CRSGLSFDST KTYQQLGHMY ADFKLVKQNI QNVDYSYVGI
510 520 530 540 550
YGWTRNPLVE FYVVDNWLSQ WRPGDWVGNK KHGDFTIDGA KYTVYENTRT
560 570 580 590 600
GPSIDGNTTF KQYFSIRQQA RDCGTIDITA HFEQWEKLGM RMGKMHEAKV
610 620
LGEAGSTGSG TSGTADFPYA KVYIK
Length:625
Mass (Da):68,049
Last modified:November 1, 1996 - v1
Checksum:i9DA99B6A17290922
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91858 mRNA. Translation: CAA62969.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91858 mRNA. Translation: CAA62969.1 .

3D structure databases

ProteinModelPortali Q12667.
SMRi Q12667. Positions 292-323.
ModBasei Search...
MobiDBi 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.
IPR013320. ConA-like_dom.
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: October 29, 2014
This is version 82 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