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Protein

Endo-1,4-beta-xylanase A

Gene

XYNA

Organism
Piromyces sp.
Status
Reviewed-Annotation score: -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: xylan degradation

This protein is involved in the pathway xylan degradation, which is part of Glycan degradation.
View all proteins of this organism that are known to be involved in the pathway xylan degradation and in Glycan degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei510NucleophilePROSITE-ProRule annotation1
Active sitei603Proton donorBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate 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 lineageiEukaryotaFungiFungi incertae sedisChytridiomycotaNeocallimastigomycetesNeocallimastigalesNeocallimastigaceaePiromyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19Sequence analysisAdd BLAST19
ChainiPRO_000000801720 – 625Endo-1,4-beta-xylanase AAdd BLAST606

Proteomic databases

PRIDEiQ12667

Structurei

3D structure databases

ProteinModelPortaliQ12667
SMRiQ12667
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 231GH11 1PROSITE-ProRule annotationAdd BLAST197
Repeati259 – 268110
Repeati269 – 278210
Domaini285 – 324CBM10 1PROSITE-ProRule annotationAdd BLAST40
Domaini332 – 371CBM10 2PROSITE-ProRule annotationAdd BLAST40
Domaini416 – 617GH11 2PROSITE-ProRule annotationAdd BLAST202

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni255 – 279LinkerAdd BLAST25
Regioni259 – 2782 X 10 AA tandem repeats of G-Q-G-[LQ]-G-N-G-Q-G-[NQ]Add BLAST20
Regioni374 – 403LinkerAdd BLAST30

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
InterProiView protein in InterPro
IPR002883 CBM10/Dockerin_dom
IPR013320 ConA-like_dom_sf
IPR009034 Dockerin_dom_fun_sf
IPR013319 GH11/12
IPR018208 GH11_AS_1
IPR033123 GH11_dom
IPR001137 Glyco_hydro_11
PfamiView protein in Pfam
PF02013 CBM_10, 2 hits
PF00457 Glyco_hydro_11, 2 hits
PRINTSiPR00911 GLHYDRLASE11
SUPFAMiSSF49899 SSF49899, 2 hits
SSF64571 SSF64571, 2 hits
PROSITEiView protein in PROSITE
PS51763 CBM10, 2 hits
PS00776 GH11_1, 1 hit
PS51761 GH11_3, 2 hits

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

Entry informationi

Entry nameiXYNA_PIRSP
AccessioniPrimary (citable) accession number: Q12667
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 23, 2018
This is version 91 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

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