P82593 (EABF_STRCX) 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): Alpha-L-AFase Extracellular arabinan exo-alpha-L-arabinosidase Short name=Arabinosidase
Organism	Streptomyces chartreusis
Taxonomic identifier	1969 [NCBI]
Taxonomic lineage	cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces

Protein attributes

Sequence length	825 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 arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of terminal alpha-L-arabinofuranosyl residues of arabinan present in the arabinofuranosyl polysaccharides or oligosaccharides. It cannot act on other arabinose-containing polysaccharides and arabinoxylo-oligosaccharides. It leaves most of the polymer intact, including most of the main-chain residues and the arabinose side chains. It acts preferentially on the linear alpha-(1->2)-linked arabinofuranobiosides and alpha-(1->3)-linked arabinofuranobiosides, and is much less effective on alpha-(1->5)-linked arabinofuranobiosides. It also hydrolyzes the terminal alpha-(1->3)-linked arabinofuranotriosides in preference to the alpha-(1->5)-linked arabinofuranotriosides. Ref.1
Catalytic activity	Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. Ref.1
Subcellular location	Secreted.
Sequence similarities	Belongs to the glycosyl hydrolase 51 family. Contains 1 CBM-cenC (cenC-type cellulose-binding) domain.
Biophysicochemical properties	pH dependence: Optimum pH is 5.5. The enzyme is slowly inactivated above pH 8.5 and below pH 5.5. Ref.1 Temperature dependence: Optimum temperature is 55 degrees Celsius. The enzyme is inactivated at temperatures above 45 degrees Celsius.

Ontologies

Keywords
Biological process	Carbohydrate metabolism
Cellular component	Secreted
Domain	Signal
Molecular function	Glycosidase Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological_process	L-arabinose metabolic process Inferred from electronic annotation. Source: InterPro
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 – 29	29	Ref.1
	Chain	30 – 825	796	Extracellular exo-alpha-L-arabinofuranosidase		PRO_0000012217
Regions
	Domain	70 – 215	146	CBM-cenC
	Region	379 – 380	2	Alpha-L-arabinofuranose binding By similarity
Sites
	Active site	380	1	Proton donor/acceptor By similarity
	Binding site	58	1	Alpha-L-arabinofuranose By similarity
	Binding site	247	1	Alpha-L-arabinofuranose; via amide nitrogen By similarity
	Site	607	1	Important for substrate recognition By similarity

Sequences

	Sequence		Length	Mass (Da)
	P82593 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 9FF4EE99BE0C696E	FASTA	825	90,184
	10 20 30 40 50 60 MSRIRWRYGT AATALLVAAG LVPTATAHAE DVTDYSITVD PAAKGAAIDD TMYGVFFEDI 70 80 90 100 110 120 NRAADGGLYA ELVQNRSFEY STDDNRSYTP LTSWIVDGTG EVVNDAGRLN ERNRNYLSLG 130 140 150 160 170 180 AGSSVTNAGY NTGIRVEQGK RYDFSVWARA GSASTLTVAL KDAAGTLATA RQVAVEGGWA 190 200 210 220 230 240 KYRATFTATR TSNRGRLAVA ANDAAALDMV SLFPRDTYRN QQNGLRKDLA EKIAALHPGF 250 260 270 280 290 300 VRFPGGCLVN TGSMEDYSAA SGWQRKRSYQ WKDTVGPVEE RATNANFWGY NQSYGLGYYE 310 320 330 340 350 360 YFRFSEDIGA MPLPVVPALV TGCGQNKAVD DEALLKRHIQ DTLDLIEFAN GPATSKWGKV 370 380 390 400 410 420 RAEMGHPRPF RLTHLEVGNE ENLPDEFFDR FKQFRAAIEA EYPDITVVSN SGPDDAGTTF 430 440 450 460 470 480 DTAWKLNREA NVEMVDEHYY NSPNWFLQNN DRYDSYDRGG PKVFLGEYAS QGNAWKNGLS 490 500 510 520 530 540 EAAFMTGLER NADVVKLASY APLLANEDYV QWRPDLVWFN NRASWNSANY EVQKLFMNNV 550 560 570 580 590 600 GDRVVPSKAT TTPDVSGPIT GAVGLSTWAT GTAYDDVKVT AADGATLLSD DFSGDASKWT 610 620 630 640 650 660 HTGAGSWSVQ DGQYVQTDAA AENTMVQAGD PSWHDYDLHV KATKKSGKEG FLVAFGVKDT 670 680 690 700 710 720 GNYYWWNLGG WNNTQSAVEQ AVDGGKGTLL TKAGSIETGR AYDIDVKVRG RQVTLYLDGQ 730 740 750 760 770 780 EWGGFTDDKP AEPFRQVVTK DARTGDLIVK VVNAQPAEAR TAIDLGGARV ASTARVTTLA 790 800 810 820 ADQDAVNTET DAPVTPATST FSGVTDRFTY TFPANSVTFL RLKQR

References

[1]

"Purification, characterization and gene cloning of two alpha-L-arabinofuranosidases from Streptomyces chartreusis GS901." Matsuo N., Kaneko S., Kuno A., Kobayashi H., Kusakabe I. Biochem. J. 346:9-15(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 30-75, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY. Strain: GS901.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB023625 Genomic DNA. Translation: BAA90771.1.
PIR	A59296.
3D structure databases
ProteinModelPortal	P82593.
ModBase	Search...
Protein family/group databases
CAZy	GH51. Glycoside Hydrolase Family 51.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR010720. Alpha-L-AF_C. IPR003305. CenC_carb-bd. IPR008985. ConA-like_lec_gl_sf. IPR008979. Galactose-bd-like. IPR017853. Glycoside_hydrolase_SF. [Graphical view]
Pfam	PF06964. Alpha-L-AF_C. 1 hit. PF02018. CBM_4_9. 1 hit. [Graphical view]
SMART	SM00813. Alpha-L-AF_C. 1 hit. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 1 hit. SSF49785. Gal_bind_like. 1 hit. SSF51445. Glyco_hydro_cat. 1 hit.
ProtoNet	Search...

Entry information

Entry name

EABF_STRCX

Accession

Primary (citable) accession number: P82593

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 17, 2003
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 57 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program