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P48790

- XYLA_CLOSR

UniProt

P48790 - XYLA_CLOSR

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Protein

Xylosidase/arabinosidase

Gene

xylA

Organism
Clostridium stercorarium
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Hydrolysis of (1->4)-beta-D-xylans, to remove successive D-xylose residues from the non-reducing termini.
Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.

GO - Molecular functioni

  1. alpha-L-arabinofuranosidase activity Source: UniProtKB-EC
  2. xylan 1,4-beta-xylosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. xylan catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Protein family/group databases

CAZyiGH43. Glycoside Hydrolase Family 43.

Names & Taxonomyi

Protein namesi
Recommended name:
Xylosidase/arabinosidase
Including the following 2 domains:
Beta-xylosidase (EC:3.2.1.37)
Alternative name(s):
1,4-beta-D-xylan xylohydrolase
Xylan 1,4-beta-xylosidase
Alpha-L-arabinofuranosidase (EC:3.2.1.55)
Short name:
Arabinosidase
Gene namesi
Name:xylA
OrganismiClostridium stercorarium
Taxonomic identifieri1510 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesRuminococcaceaeRuminiclostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 473473Xylosidase/arabinosidasePRO_0000057695Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Structurei

3D structure databases

ProteinModelPortaliP48790.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 43 family.Curated

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
2.60.120.260. 1 hit.
InterProiIPR008979. Galactose-bd-like.
IPR006710. Glyco_hydro_43.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PANTHERiPTHR22925. PTHR22925. 1 hit.
PfamiPF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
SUPFAMiSSF75005. SSF75005. 1 hit.

Sequencei

Sequence statusi: Complete.

P48790-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRKQRFNPYL PSWEYIPDAE PYVFNGRVYI YGSHDRFNGH AFCLNDYVCW
60 70 80 90 100
SAPVDDLSEW RYEGVIYRKT DDPLNPDGRM CLYAPDVTLG PDGRYYLYYV
110 120 130 140 150
LDKVPVVSVA VCDTPAGKYE FYGYVRYADG TRLGEREGDW PQFDPAVLTE
160 170 180 190 200
GERTYLYTGF CPKGDKSRKG AMATVLGPDM LTVVEEPVII VPSEPYSRGS
210 220 230 240 250
GFEGHEFFEA PSIRKKGDTY YFIYSSVVMH ELCYATSKHP TKGFKYGGVI
260 270 280 290 300
VSNCDLHIDS YKPAEKPMYY GGNNHGSIVE INGEWYIFYH RHTNGTSFSR
310 320 330 340 350
QGCMEKIKIL EDGSIPQVEM TSCGSADEPL PGRGEYPAYI ACNLFCGEES
360 370 380 390 400
VYTDLTGAWM NNQFPKITQD GKDGDEEPGY IANMKDSATA GFKYFDCKGI
410 420 430 440 450
KSVKIKVRGY CRGVFEVKTS WNGEVLGKIP VEFSNIWTEF SASIPIPDGI
460 470
HALYFTYRGS GSASLKSFTL CTD
Length:473
Mass (Da):53,341
Last modified:February 1, 1996 - v1
Checksum:iCDA34CE9DEBB2399
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D13268 Genomic DNA. Translation: BAA02527.1.
PIRiJQ1936.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D13268 Genomic DNA. Translation: BAA02527.1 .
PIRi JQ1936.

3D structure databases

ProteinModelPortali P48790.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GH43. Glycoside Hydrolase Family 43.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 2.115.10.20. 1 hit.
2.60.120.260. 1 hit.
InterProi IPR008979. Galactose-bd-like.
IPR006710. Glyco_hydro_43.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view ]
PANTHERi PTHR22925. PTHR22925. 1 hit.
Pfami PF04616. Glyco_hydro_43. 1 hit.
[Graphical view ]
SUPFAMi SSF75005. SSF75005. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence of the Clostridium stercorarium xylA gene encoding a bifunctional protein with beta-D-xylosidase and alpha-L-arabinofuranosidase activities, and properties of the translated product."
    Sakka K., Yoshikawa K., Kojima Y., Karita S., Ohmiya K., Shimada K.
    Biosci. Biotechnol. Biochem. 57:268-272(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.

Entry informationi

Entry nameiXYLA_CLOSR
AccessioniPrimary (citable) accession number: P48790
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: October 1, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing, Multifunctional enzyme

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3