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Protein

Exo-1,4-beta-xylosidase xlnD

Gene

xlnD

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Xylan 1,4-beta-xylosidase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.2 Publications

Catalytic activityi

Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.

pH dependencei

Optimum pH is 5.1.1 Publication

Temperature dependencei

Optimum temperature is 52 degrees Celsius.1 Publication

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 sitei307By similarity1

GO - Molecular functioni

  • alpha-L-arabinofuranosidase activity Source: GO_Central
  • xylan 1,4-beta-xylosidase activity Source: UniProtKB

GO - Biological processi

  • arabinan catabolic process Source: GO_Central
  • xylan catabolic process Source: UniProtKB
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

CAZyiGH3. Glycoside Hydrolase Family 3.
mycoCLAPiXYL3C_EMENI.

Names & Taxonomyi

Protein namesi
Recommended name:
Exo-1,4-beta-xylosidase xlnD (EC:3.2.1.37)
Alternative name(s):
1,4-beta-D-xylan xylohydrolase xlnD
Beta-xylosidase A
Beta-xylosidase xlnD
Xylobiase xlnD
Gene namesi
Name:xlnD
Synonyms:xylA
ORF Names:AN2359
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000000560 Componenti: Chromosome VII
  • UP000005890 Componenti: Partially assembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18Sequence analysisAdd BLAST18
ChainiPRO_000039329319 – 803Exo-1,4-beta-xylosidase xlnDAdd BLAST785

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi21N-linked (GlcNAc...)Sequence analysis1
Glycosylationi44N-linked (GlcNAc...)Sequence analysis1
Glycosylationi85N-linked (GlcNAc...)Sequence analysis1
Glycosylationi122N-linked (GlcNAc...)Sequence analysis1
Glycosylationi140N-linked (GlcNAc...)Sequence analysis1
Glycosylationi234N-linked (GlcNAc...)Sequence analysis1
Glycosylationi437N-linked (GlcNAc...)Sequence analysis1
Glycosylationi474N-linked (GlcNAc...)Sequence analysis1
Glycosylationi515N-linked (GlcNAc...)Sequence analysis1
Glycosylationi611N-linked (GlcNAc...)Sequence analysis1
Glycosylationi676N-linked (GlcNAc...)Sequence analysis1
Glycosylationi698N-linked (GlcNAc...)Sequence analysis1

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ5BAS1.

Structurei

3D structure databases

ProteinModelPortaliQ5BAS1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 3 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000031216.
InParanoidiQ5BAS1.
KOiK15920.
OMAiRVEMGID.
OrthoDBiEOG092C1FFP.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProiIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR30620. PTHR30620. 1 hit.
PfamiPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
SMARTiSM01217. Fn3_like. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q5BAS1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSLISVAVL SALPTAFSQA NTSYTDYNVE ANPDLFPLCL QHLNASFPDC
60 70 80 90 100
ASGPLSLTPV CDRSLSPKDR ATALVSLFTF DELVNNTGNT GLGVSRLGLP
110 120 130 140 150
NYQVWGEALH GVGRANFVES GNFSWATSFP MPITMMAALN KTLIHQIGTI
160 170 180 190 200
VSTQLRAFSN AGLGGVDVYS PNINTFRHPV WGRGQETPGE DAFLTSVYGY
210 220 230 240 250
EYITALQGGV DPETLKIIAT AKHYAGYDIE SWNNHSRLGN DMQITQQELS
260 270 280 290 300
EYYTPPFIVA SRDAKVRSVM CSYNAVNGVP SCANKFFLQT LLRDTFEFSE
310 320 330 340 350
DGYVSGDCGA VYNVWNPHGY ASNEAAASAD SILAGTDIDC GTSYQWHSED
360 370 380 390 400
AFEDSLVSRS DIERGVIRLY SNLVQAGYFD GEDAPYRDIT WDDVLSTDAW
410 420 430 440 450
NIAYEAAVEG IVLLKNDETL PLSKDIKSVA VIGPWANVTE ELQGNYFGPA
460 470 480 490 500
PYLISPLTGF RDSGLDVHYA LGTNLTSHST SGFEEALTAA KQADAIIFAG
510 520 530 540 550
GIDNTIEAEA MDRENITWPG NQLDLISKLS ELGKPLVVLQ MGGGQVDSSS
560 570 580 590 600
LKDNDNVNAL IWGGYPGQSG GHALADIITG KRAPAGRLVT TQYPAEYAEV
610 620 630 640 650
FPAIDMNLRP NETSGNPGQT YMWYTGTPVY EFGHGLFYTT FEESTETTDA
660 670 680 690 700
GSFNIQTVLT TPHSGYEHAQ QKTLLNFTAT VKNTGERESD YTALVYVNTT
710 720 730 740 750
AGPAPYPKKW VVGFDRLGGL EPGDSQTLTV PVTVESVART DEQGNRVLYP
760 770 780 790 800
GSYELALNNE RSVVVKFELK GEEAVILSWP EDTTSDFVSS IDGGLDRKQD

VIA
Length:803
Mass (Da):87,196
Last modified:April 26, 2005 - v1
Checksum:i9EF12F7391B043B2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti14 – 15PT → A in CAA73902 (PubMed:9546179).Curated2
Sequence conflicti52S → T in CAA73902 (PubMed:9546179).Curated1
Sequence conflicti209G → A in CAA73902 (PubMed:9546179).Curated1
Sequence conflicti215L → S in CAA73902 (PubMed:9546179).Curated1
Sequence conflicti754 – 755EL → DV in CAA73902 (PubMed:9546179).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13568 Genomic DNA. Translation: CAA73902.1.
AACD01000039 Genomic DNA. Translation: EAA64470.1.
BN001307 Genomic DNA. Translation: CBF86686.1.
RefSeqiXP_659963.1. XM_654871.1.

Genome annotation databases

EnsemblFungiiCADANIAT00009060; CADANIAP00009060; CADANIAG00009060.
EAA64470; EAA64470; AN2359.2.
GeneIDi2875035.
KEGGiani:AN2359.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13568 Genomic DNA. Translation: CAA73902.1.
AACD01000039 Genomic DNA. Translation: EAA64470.1.
BN001307 Genomic DNA. Translation: CBF86686.1.
RefSeqiXP_659963.1. XM_654871.1.

3D structure databases

ProteinModelPortaliQ5BAS1.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH3. Glycoside Hydrolase Family 3.
mycoCLAPiXYL3C_EMENI.

Proteomic databases

PRIDEiQ5BAS1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00009060; CADANIAP00009060; CADANIAG00009060.
EAA64470; EAA64470; AN2359.2.
GeneIDi2875035.
KEGGiani:AN2359.2.

Phylogenomic databases

HOGENOMiHOG000031216.
InParanoidiQ5BAS1.
KOiK15920.
OMAiRVEMGID.
OrthoDBiEOG092C1FFP.

Enzyme and pathway databases

UniPathwayiUPA00114.

Family and domain databases

Gene3Di3.20.20.300. 1 hit.
3.40.50.1700. 1 hit.
InterProiIPR026891. Fn3-like.
IPR026892. Glyco_hydro_3.
IPR002772. Glyco_hydro_3_C.
IPR001764. Glyco_hydro_3_N.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PANTHERiPTHR30620. PTHR30620. 1 hit.
PfamiPF14310. Fn3-like. 1 hit.
PF00933. Glyco_hydro_3. 1 hit.
PF01915. Glyco_hydro_3_C. 1 hit.
[Graphical view]
SMARTiSM01217. Fn3_like. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
SSF52279. SSF52279. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiXYND_EMENI
AccessioniPrimary (citable) accession number: Q5BAS1
Secondary accession number(s): C8VNG4, O42810
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 23, 2010
Last sequence update: April 26, 2005
Last modified: September 7, 2016
This is version 71 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

Complete proteome, Reference proteome

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

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.