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P96463

- EABF_STRLI

UniProt

P96463 - EABF_STRLI

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Protein

Extracellular exo-alpha-L-arabinofuranosidase

Gene
abfB
Organism
Streptomyces lividans
Status
Reviewed - 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)

Vmax=17.2 µmol/min/mg enzyme with oat xylan as substrate (at 55 degrees Celsius)

Vmax=18.5 µmol/min/mg enzyme with wheat arabinoxylan as substrate (at 55 degrees Celsius)

pH dependencei

Optimum pH is 6.

Temperature dependencei

Optimum temperature is 55 degrees Celsius.

Pathwayi

GO - Molecular functioni

  1. alpha-L-arabinofuranosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. L-arabinose metabolic process Source: InterPro
  2. xylan catabolic process Source: UniProtKB-UniPathway
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

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

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

Structurei

3D structure databases

ProteinModelPortaliP96463.
SMRiP96463. Positions 38-164.

Family & Domainsi

Domains and Repeats

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

Sequence similaritiesi

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

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MHRGSLSRGQ HVRGTRRRGA ALAALAALLV ATAPAQAAGS GALRGAGSNR    50
CLDVLGGSQD DGALLQLYDC WGGTNQQWTS TDTGRLTVYG DKCLDVPGHA 100
TAPGTRVQIW SCSGGRNQQW RVNSDGTVVG VESGLCLEAA GAGTPNGTAV 150
QLWTCNGGGN QKWTGLTGTP PTDGTCALPS TYRWSSTGVL AQPKSGWVAL 200
KDFTTVTHNG RHLVYGSTSS GSSYGSMVFS PFTNWSDMAS AGQNAMNQAA 250
VAPTLFYFAP KNIWVLAYQW GSWPFIYRTS SDPTDPNGWS APQPLFTGSI 300
SGSDTGPIDQ TLIADGQNMY LFFAGDNGKI YRASMPIGNF PGNFGSSYTT 350
IMSDTKANLF EGVQVYKVQG QNQYLMIVEA MGANGRYFRS FTASSLSGSW 400
TPQAASEGNP FAGKANSGAT WTNDISHGDL VRDNPDQTMT VDPCNLQFLY 450
QGKAPNAGGH YNSLPWRPGV LTLRH 475
Length:475
Mass (Da):50,369
Last modified:December 15, 1998 - v2
Checksum:iC3CB14EE7BF85AAD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64551 Genomic DNA. Translation: AAC26524.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M64551 Genomic DNA. Translation: AAC26524.1 .

3D structure databases

ProteinModelPortali P96463.
SMRi P96463. Positions 38-164.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM13. Carbohydrate-Binding Module Family 13.
GH62. Glycoside Hydrolase Family 62.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Enzyme and pathway databases

UniPathwayi UPA00114 .

Family and domain databases

InterProi IPR005193. GH62_arabinosidase.
IPR023296. Glyco_hydro_beta-prop.
IPR000772. Ricin_B_lectin.
[Graphical view ]
Pfami PF03664. Glyco_hydro_62. 1 hit.
PF00652. Ricin_B_lectin. 1 hit.
[Graphical view ]
SMARTi SM00458. RICIN. 1 hit.
[Graphical view ]
SUPFAMi SSF50370. SSF50370. 1 hit.
SSF75005. SSF75005. 1 hit.
PROSITEi PS50231. RICIN_B_LECTIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: May 14, 2014
This is version 80 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 (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

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