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P29127

- XYNA_NEOPA

UniProt

P29127 - XYNA_NEOPA

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Protein

Bifunctional endo-1,4-beta-xylanase A

Gene

XYNA

Organism
Neocallimastix patriciarum (Rumen fungus)
Status
Reviewed - 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei141 – 1411NucleophilePROSITE-ProRule annotation
Active sitei223 – 2231Proton donorPROSITE-ProRule annotation
Active sitei386 – 3861NucleophilePROSITE-ProRule annotation
Active sitei474 – 4741Proton donorPROSITE-ProRule annotation

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

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)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 607589Bifunctional endo-1,4-beta-xylanase APRO_0000008016Add
BLAST

Structurei

Secondary structure

1
607
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi275 – 2817Combined sources
Beta strandi283 – 2897Combined sources
Beta strandi292 – 2976Combined sources
Beta strandi305 – 3095Combined sources
Beta strandi315 – 3206Combined sources
Beta strandi327 – 3359Combined sources
Helixi342 – 3443Combined sources
Beta strandi345 – 37531Combined sources
Beta strandi385 – 39511Combined sources
Beta strandi403 – 4075Combined sources
Beta strandi410 – 42314Combined sources
Beta strandi426 – 44015Combined sources
Beta strandi443 – 4486Combined sources
Helixi449 – 4579Combined sources
Turni458 – 4603Combined sources
Beta strandi468 – 49225Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C1FX-ray2.10A275-499[»]
2VG9X-ray2.00A275-492[»]
ProteinModelPortaliP29127.
SMRiP29127. Positions 30-247, 275-492, 529-562, 572-605.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29127.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini524 – 56239CBM10 1Add
BLAST
Domaini566 – 60540CBM10 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 255226Catalytic 1Add
BLAST
Regioni275 – 499225Catalytic 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi256 – 27419Ser/Thr-rich (linker)Add
BLAST
Compositional biasi500 – 52324Ser/Thr-rich (linker)Add
BLAST

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. 2 hits.
PS00777. GLYCOSYL_HYDROL_F11_2. 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 .
PIRi S24754.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C1F X-ray 2.10 A 275-499 [» ]
2VG9 X-ray 2.00 A 275-492 [» ]
ProteinModelPortali P29127.
SMRi P29127. Positions 30-247, 275-492, 529-562, 572-605.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH11. Glycoside Hydrolase Family 11.
mycoCLAPi XYN11A_NEOPA.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00114 .
BRENDAi 3.2.1.8. 6834.

Miscellaneous databases

EvolutionaryTracei P29127.

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. 2 hits.
PS00777. GLYCOSYL_HYDROL_F11_2. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Homologous catalytic domains in a rumen fungal xylanase: evidence for gene duplication and prokaryotic origin."
    Gilbert H.J., Hazlewood G.P., Laurie J.I., Orpin C.G., Xue G.P.
    Mol. Microbiol. 6:2065-2072(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

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 26, 2014
This is version 101 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

External Data

Dasty 3