P96463 (EABF_STRLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Extracellular exo-alpha-L-arabinofuranosidase
Short name=ABF
EC=3.2.1.55

Alternative name(s):
Arabinosidase
Arabinoxylan arabinofuranohydrolase

Gene names

Name:

abfB

Organism

Streptomyces lividans

Taxonomic identifier

1916 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	475 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1
Catalytic activity	Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. Ref.1
Pathway	Glycan degradation; xylan degradation.
Subcellular location	Secreted Ref.1.
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 (Ref.1).
Sequence similarities	Belongs to the glycosyl hydrolase 62 family. Contains 1 ricin B-type lectin domain.
Biophysicochemical properties	Kinetic parameters: KM=1.17 mM for wheat arabinoxylan (at 55 degrees Celsius) Ref.1 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 dependence: Optimum pH is 6. Temperature dependence: Optimum temperature is 55 degrees Celsius.

Ontologies

Keywords
Biological process	Xylan degradation
Cellular component	Secreted
Domain	Signal
Ligand	Lectin
Molecular function	Glycosidase Hydrolase
Gene Ontology (GO)
Biological_process	L-arabinose metabolic process Inferred from electronic annotation. Source: InterPro xylan catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	alpha-N-arabinofuranosidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 37	37	Potential
	Chain	38 – 475	438	Extracellular exo-alpha-L-arabinofuranosidase		PRO_0000008037
Regions
	Domain	39 – 166	128	Ricin B-type lectin

Sequences

	Sequence		Length	Mass (Da)
	P96463 [UniParc]. Last modified December 15, 1998. Version 2. Checksum: C3CB14EE7BF85AAD	FASTA	475	50,369
	10 20 30 40 50 60 MHRGSLSRGQ HVRGTRRRGA ALAALAALLV ATAPAQAAGS GALRGAGSNR CLDVLGGSQD 70 80 90 100 110 120 DGALLQLYDC WGGTNQQWTS TDTGRLTVYG DKCLDVPGHA TAPGTRVQIW SCSGGRNQQW 130 140 150 160 170 180 RVNSDGTVVG VESGLCLEAA GAGTPNGTAV QLWTCNGGGN QKWTGLTGTP PTDGTCALPS 190 200 210 220 230 240 TYRWSSTGVL AQPKSGWVAL KDFTTVTHNG RHLVYGSTSS GSSYGSMVFS PFTNWSDMAS 250 260 270 280 290 300 AGQNAMNQAA VAPTLFYFAP KNIWVLAYQW GSWPFIYRTS SDPTDPNGWS APQPLFTGSI 310 320 330 340 350 360 SGSDTGPIDQ TLIADGQNMY LFFAGDNGKI YRASMPIGNF PGNFGSSYTT IMSDTKANLF 370 380 390 400 410 420 EGVQVYKVQG QNQYLMIVEA MGANGRYFRS FTASSLSGSW TPQAASEGNP FAGKANSGAT 430 440 450 460 470 WTNDISHGDL VRDNPDQTMT VDPCNLQFLY QGKAPNAGGH YNSLPWRPGV LTLRH

References

[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.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M64551 Genomic DNA. Translation: AAC26524.1.
3D structure databases
ProteinModelPortal	P96463.
SMR	P96463. Positions 38-164.
ModBase	Search...
Protein family/group databases
CAZy	CBM13. Carbohydrate-Binding Module Family 13. GH62. Glycoside Hydrolase Family 62.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
UniPathway	UPA00114.
Family and domain databases
InterPro	IPR005193. GH62_arabinosidase. IPR023296. Glyco_hydro_beta-prop. IPR000772. Ricin_B_lectin. [Graphical view]
Pfam	PF03664. Glyco_hydro_62. 1 hit. PF00652. Ricin_B_lectin. 1 hit. [Graphical view]
SMART	SM00458. RICIN. 1 hit. [Graphical view]
SUPFAM	SSF75005. Glyco_hydro_43_beta-prop. 1 hit. SSF50370. RicinB_like. 1 hit.
PROSITE	PS50231. RICIN_B_LECTIN. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

EABF_STRLI

Accession

Primary (citable) accession number: P96463

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 15, 1998
Last sequence update:	December 15, 1998
Last modified:	May 1, 2013
This is version 77 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program