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Protein

Bifunctional endo-1,4-beta-xylanase A

Gene

XYNA

Organism
Neocallimastix patriciarum (Rumen fungus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes xylans into xylobiose and xylose.

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 sitei141NucleophilePROSITE-ProRule annotation1
Active sitei223Proton donorPROSITE-ProRule annotation1
Active sitei386NucleophilePROSITE-ProRule annotation1
Active sitei474Proton donorPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

BRENDAi3.2.1.8. 6834.
UniPathwayiUPA00114.

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11A_NEOPA.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional endo-1,4-beta-xylanase A (EC:3.2.1.8)
Short name:
XYLA
Gene namesi
Name:XYNA
OrganismiNeocallimastix patriciarum (Rumen fungus)
Taxonomic identifieri4758 [NCBI]
Taxonomic lineageiEukaryotaFungiNeocallimastigomycotaNeocallimastigomycetesNeocallimastigalesNeocallimastigaceaeNeocallimastix

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000000801619 – 607Bifunctional endo-1,4-beta-xylanase AAdd BLAST589

Proteomic databases

PRIDEiP29127.

Structurei

Secondary structure

1607
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi275 – 281Combined sources7
Beta strandi283 – 289Combined sources7
Beta strandi292 – 297Combined sources6
Beta strandi305 – 309Combined sources5
Beta strandi315 – 320Combined sources6
Beta strandi327 – 335Combined sources9
Helixi342 – 344Combined sources3
Beta strandi345 – 375Combined sources31
Beta strandi385 – 395Combined sources11
Beta strandi403 – 407Combined sources5
Beta strandi410 – 423Combined sources14
Beta strandi426 – 440Combined sources15
Beta strandi443 – 448Combined sources6
Helixi449 – 457Combined sources9
Turni458 – 460Combined sources3
Beta strandi468 – 492Combined sources25

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2C1FX-ray2.10A275-499[»]
2VG9X-ray2.00A275-492[»]
ProteinModelPortaliP29127.
SMRiP29127.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29127.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 242GH11 1PROSITE-ProRule annotationAdd BLAST208
Domaini280 – 487GH11 2PROSITE-ProRule annotationAdd BLAST208
Domaini523 – 563CBM10 1PROSITE-ProRule annotationAdd BLAST41
Domaini566 – 606CBM10 2PROSITE-ProRule annotationAdd BLAST41

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi256 – 274Ser/Thr-rich (linker)Add BLAST19
Compositional biasi500 – 523Ser/Thr-rich (linker)Add BLAST24

Sequence similaritiesi

Contains 2 CBM10 (carbohydrate binding type-10) domains.PROSITE-ProRule annotationCurated
Contains 2 GH11 (glycosyl hydrolase family 11) domains.PROSITE-ProRule annotation

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.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR001137. Glyco_hydro_11.
[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.
PROSITEiPS51763. CBM10. 2 hits.
PS00776. GH11_1. 2 hits.
PS00777. GH11_2. 2 hits.
PS51761. GH11_3. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P29127-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTIKFFFAV AIATVAKAQW GGGGASAGQR LTVGNGQTQH KGVADGYSYE
60 70 80 90 100
IWLDNTGGSG SMTLGSGATF KAEWNASVNR GNFLARRGLD FGSQKKATDY
110 120 130 140 150
SYIGLDYTAT YRQTGSASGN SRLCVYGWFQ NRGVQGVPLV EYYIIEDWVD
160 170 180 190 200
WVSDAQGRMV TIDGAQYKIF QMDHTGPTIN GGSETFKQYF SVRQQKRTSG
210 220 230 240 250
HITVSDHFKE WAKQGWGIGN LYEVALNAEG WQSSGIADVT KLDVYTTQKG
260 270 280 290 300
SNPAPTSTGT VPSSSAGGST ANGKKFTVGN GQNQHKGVND GFSYEIWLDN
310 320 330 340 350
TGGNGSMTLG SGATFKAEWN AAVNRGNFLA RRGLDFGSQK KATDYDYIGL
360 370 380 390 400
DYAATYKQTA SASGNSRLCV YGWFQNRGLN GVPLVEYYII EDWVDWVPDA
410 420 430 440 450
QGKMVTIDGA QYKIFQMDHT GPTINGGSET FKQYFSVRQQ KRTSGHITVS
460 470 480 490 500
DHFKEWAKQG WGIGNLYEVA LNAEGWQSSG VADVTLLDVY TTPKGSSPAT
510 520 530 540 550
SAAPRTTTRT TTRTKSLPTN YNKCSARITA QGYKCCSDPN CVVYYTDEDG
560 570 580 590 600
TWGVENNDWC GCGVEQCSSK ITSQGYKCCS DPNCVVFYTD DDGKWGVENN

DWCGCGF
Length:607
Mass (Da):66,175
Last modified:December 1, 1992 - v1
Checksum:i9C5B73A67D0CC780
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65526 mRNA. Translation: CAA46498.1.
PIRiS24754.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65526 mRNA. Translation: CAA46498.1.
PIRiS24754.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2C1FX-ray2.10A275-499[»]
2VG9X-ray2.00A275-492[»]
ProteinModelPortaliP29127.
SMRiP29127.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH11. Glycoside Hydrolase Family 11.
mycoCLAPiXYN11A_NEOPA.

Proteomic databases

PRIDEiP29127.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.
BRENDAi3.2.1.8. 6834.

Miscellaneous databases

EvolutionaryTraceiP29127.

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.
IPR013319. GH11/12.
IPR018208. GH11_AS_1.
IPR033119. GH11_AS_2.
IPR033123. GH11_dom.
IPR001137. Glyco_hydro_11.
[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.
PROSITEiPS51763. CBM10. 2 hits.
PS00776. GH11_1. 2 hits.
PS00777. GH11_2. 2 hits.
PS51761. GH11_3. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXYNA_NEOPA
AccessioniPrimary (citable) accession number: P29127
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: November 2, 2016
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Multifunctional enzyme

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.