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P53627 (IABF_STRLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Intracellular exo-alpha-(1->5)-L-arabinofuranosidase

Short name=ABF
EC=3.2.1.55
Alternative name(s):
Alpha-L-AF
Arabinoxylan arabinofuranohydrolase
Intracellular arabinan exo-alpha-(1->5)-L-arabinosidase
Short name=Arabinosidase
Gene names
Name:abfA
OrganismStreptomyces lividans
Taxonomic identifier1916 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length662 AA.
Sequence statusComplete.
Protein existenceEvidence 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-(1->5)-arabinofuranosyl bonds in different hemicellulosic homopolysaccharides (arabino-oligoxylosides, branched and debranched arabinans). It acts rapidly on the short-chain arabino-oligoxylosides from digestion of xylan with xylanases. It hydrolyzes slowly arabinan and arabinoxylan from wheat and rye flour. Ref.1

Catalytic activity

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

Pathway

Glycan metabolism; L-arabinan degradation.

Subunit structure

Homohexamer; trimer of dimers Probable. Ref.1

Subcellular location

Cytoplasm Ref.1.

Sequence similarities

Belongs to the glycosyl hydrolase 51 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.6 mM for p-nitrophenyl alpha-L-arabinofuranoside (pNP-Araf) (at 60 degrees Celsius and at pH 6) Ref.1

Vmax=180 µmol/min/mg enzyme (at 60 degrees Celsius and at pH 6)

pH dependence:

Optimum pH is 6.0.

Temperature dependence:

Optimum temperature is 60 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processL-arabinose metabolic process

Inferred from electronic annotation. Source: InterPro

arabinan catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionalpha-L-arabinofuranosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 662662Intracellular exo-alpha-(1->5)-L-arabinofuranosidase
PRO_0000057704

Regions

Region174 – 1752Substrate binding By similarity

Sites

Active site1751Proton donor/acceptor By similarity
Active site2941Nucleophile By similarity
Binding site271Substrate By similarity
Binding site721Substrate; via amide nitrogen By similarity
Binding site2461Substrate By similarity
Binding site2941Substrate By similarity
Binding site3521Substrate By similarity
Site2981Important for substrate recognition By similarity
Site3521Important for substrate recognition By similarity

Sequences

Sequence LengthMass (Da)Tools
P53627 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: DAAF66A577C1D6D1

FASTA66272,497
        10         20         30         40         50         60 
MRTARFTLDP AFTVGAVNPR LFGSFVEHLG RCVYTGVFEP GHPTADAEGL RQDVLELVRE 

        70         80         90        100        110        120 
LGVTAVRYPG GNFVSGYKWE DSVGPVEDRP RRLDLAWRST ETNRFGLSEY IAFLKKIGPQ 

       130        140        150        160        170        180 
AEPMMAVNLG TRGVAEALEL QEYANHPSGT ALSDLRAEHG DKDPFGIRLW CLGNEMDGPW 

       190        200        210        220        230        240 
QTGHKTAEEY GRVAAETARA MRQIDPDVEL VACGSSGQSM ETFAEWEATV LKETYDLVDH 

       250        260        270        280        290        300 
ISLHAYYEPH DGDVDSFLAS AVDMESFIEN VVATCDHVGA RLKSKKKINL SFDEWNVWYM 

       310        320        330        340        350        360 
TKTQAEVSAL DWPEAPRLLE DNYSVMDAVV FGSLLIALLR HADRVTVACL AQLVNVIAPI 

       370        380        390        400        410        420 
MTEPGGPAWR QTTFFPFSQA SKYGRGEVLD VRVDSPTYDT AKYGEADLLH ATAVVRARRS 

       430        440        450        460        470        480 
VTVFAVNRSR TGALPLEVAL SGLELTEVVE HSALADADPD ARNTLAEPER VVPHPVDGTS 

       490        500        510        520        530        540 
LRDGRLTAAL EPLSWNSIRC ADPAPGQPPR RPGEGTGFTG TPPAAPPSSS SAPRPDPTAR 

       550        560        570        580        590        600 
RSPDRTARAR VLAAARVRRM PFGRTKVCGA PVRPPTYAPR FQPFRKTWTR WAPAPRSGSP 

       610        620        630        640        650        660 
SRRSPTEASI PGGTSSRNVV RYQVTPWRRS PPGSAPGTPA PTRRRRTRAG ASRGAPRTAR 


RC 

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References

[1]"Purification and characterization of an alpha-L-arabinofuranosidase from Streptomyces lividans 66 and DNA sequence of the gene (abfA)."
Manin C., Shareek F., Morosoli R., Kluepfel D.
Biochem. J. 302:443-449(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-23, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, SUBSTRATE SPECIFICITY, SUBUNIT.
Strain: 66 / 1326.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U04630 Genomic DNA. Translation: AAA61708.1.
PIRS55274.

3D structure databases

ProteinModelPortalP53627.
SMRP53627. Positions 3-500.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH51. Glycoside Hydrolase Family 51.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00667.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR010720. Alpha-L-AF_C.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF06964. Alpha-L-AF_C. 1 hit.
[Graphical view]
SMARTSM00813. Alpha-L-AF_C. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameIABF_STRLI
AccessionPrimary (citable) accession number: P53627
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries