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Protein

Extracellular exo-alpha-L-arabinofuranosidase

Gene

abfB

Organism
Streptomyces lividans
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the degradation of xylan and is a key enzyme in the complete degradation of the plant cell wall. It has a specific arabinofuranose-debranching activity on xylan from gramineae. Acts synergistically with the xylanases and binds specifically to xylan. From small arabinoxylo-oligosides (ranging from arabinoxylotriose to arabinoxylohexaose), it liberates arabinose and, after prolonged incubation, the purified enzyme exhibits some xylanolytic activity as well.1 Publication

Catalytic activityi

Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides.1 Publication

Kineticsi

  1. KM=1.17 mM for wheat arabinoxylan (at 55 degrees Celsius)1 Publication
  2. KM=5.12 mM for oat xylan (at 55 degrees Celsius)1 Publication
  1. Vmax=17.2 µmol/min/mg enzyme with oat xylan as substrate (at 55 degrees Celsius)1 Publication
  2. Vmax=18.5 µmol/min/mg enzyme with wheat arabinoxylan as substrate (at 55 degrees Celsius)1 Publication

pH dependencei

Optimum pH is 6.1 Publication

Temperature dependencei

Optimum temperature is 55 degrees Celsius.1 Publication

Pathwayi

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Keywords - Ligandi

Lectin

Enzyme and pathway databases

UniPathwayiUPA00114.

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GH62. Glycoside Hydrolase Family 62.

Names & Taxonomyi

Protein namesi
Recommended name:
Extracellular exo-alpha-L-arabinofuranosidase (EC:3.2.1.55)
Short name:
ABF
Alternative name(s):
Arabinosidase
Arabinoxylan arabinofuranohydrolase
Gene namesi
Name:abfB
OrganismiStreptomyces lividans
Taxonomic identifieri1916 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3737Sequence AnalysisAdd
BLAST
Chaini38 – 475438Extracellular exo-alpha-L-arabinofuranosidasePRO_0000008037Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP96463.
SMRiP96463. Positions 38-164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 166128Ricin B-type lectinPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glycosyl hydrolase 62 family.Curated
Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR005193. GH62_arabinosidase.
IPR023296. Glyco_hydro_beta-prop.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF03664. Glyco_hydro_62. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P96463-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHRGSLSRGQ HVRGTRRRGA ALAALAALLV ATAPAQAAGS GALRGAGSNR
60 70 80 90 100
CLDVLGGSQD DGALLQLYDC WGGTNQQWTS TDTGRLTVYG DKCLDVPGHA
110 120 130 140 150
TAPGTRVQIW SCSGGRNQQW RVNSDGTVVG VESGLCLEAA GAGTPNGTAV
160 170 180 190 200
QLWTCNGGGN QKWTGLTGTP PTDGTCALPS TYRWSSTGVL AQPKSGWVAL
210 220 230 240 250
KDFTTVTHNG RHLVYGSTSS GSSYGSMVFS PFTNWSDMAS AGQNAMNQAA
260 270 280 290 300
VAPTLFYFAP KNIWVLAYQW GSWPFIYRTS SDPTDPNGWS APQPLFTGSI
310 320 330 340 350
SGSDTGPIDQ TLIADGQNMY LFFAGDNGKI YRASMPIGNF PGNFGSSYTT
360 370 380 390 400
IMSDTKANLF EGVQVYKVQG QNQYLMIVEA MGANGRYFRS FTASSLSGSW
410 420 430 440 450
TPQAASEGNP FAGKANSGAT WTNDISHGDL VRDNPDQTMT VDPCNLQFLY
460 470
QGKAPNAGGH YNSLPWRPGV LTLRH
Length:475
Mass (Da):50,369
Last modified:December 15, 1998 - v2
Checksum:iC3CB14EE7BF85AAD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64551 Genomic DNA. Translation: AAC26524.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64551 Genomic DNA. Translation: AAC26524.1.

3D structure databases

ProteinModelPortaliP96463.
SMRiP96463. Positions 38-164.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.
GH62. Glycoside Hydrolase Family 62.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00114.

Family and domain databases

InterProiIPR005193. GH62_arabinosidase.
IPR023296. Glyco_hydro_beta-prop.
IPR000772. Ricin_B_lectin.
[Graphical view]
PfamiPF03664. Glyco_hydro_62. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]
SMARTiSM00458. RICIN. 1 hit.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEiPS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "New alpha-L-arabinofuranosidase produced by Streptomyces lividans: cloning and DNA sequence of the abfB gene and characterization of the enzyme."
    Vincent P., Shareck F., Dupont C., Morosoli R., Kluepfel D.
    Biochem. J. 322:845-852(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, SUBSTRATE SPECIFICITY.
    Strain: 66 / 1326.
  2. Shareck F.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.

Entry informationi

Entry nameiEABF_STRLI
AccessioniPrimary (citable) accession number: P96463
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: January 7, 2015
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

These dual activities might be explained by a rotation about the alpha-(1->3)-glycosidic bond of the arabinofuranose group to the xylose moiety of xylan, which produces a bond conformation resembling that of a beta-(1->4) bond found in xylosides. Thus a single catalytic site could perform the double activity (PubMed:9148759).1 Publication

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

External Data

Dasty 3

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 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.