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P94552 (IABF2_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
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-L-arabinofuranosidase 2
Short name=ABF
EC=3.2.1.55
Alternative name(s):
Intracellular arabinan exo-alpha-L-arabinosidase
Short name=Arabinosidase
Gene names
Name:abf2
Synonyms:asd, xsa
Ordered Locus Names:BSU28510
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length495 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 cleveage of terminal alpha-L-arabinofuranosyl residues in different hemicellulosic homopolysaccharides (branched and debranched arabinans) and heteropolysaccharides (arabinoxylans). It is able to hydrolyze the alpha-(1->5)-glycosidic linkages of linear alpha-(1->5)-L-arabinan (debranched), sugar beet arabinan (branched) and wheat arabinoxylan. Moreover, it displays higher activity towards branched arabinan, a molecule comprising a backbone of alpha-(1->5)-linked L-arabinofuranosyl residues decorated with alpha-(1->2)-, and alpha-(1->3)-linked L-arabinofuranosyl units, than towards debranched arabinan. In addition, arabinoxylan, which has L-arabinofuranose residues attached to the main chain by alpha-(1->2)-and/or alpha-(1->3)-glycosidic linkages, is preferred to linear alpha-(1->5)-L-arabinan. Ref.3

Catalytic activity

Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides. Ref.3

Pathway

Glycan metabolism; L-arabinan degradation.

Subunit structure

Homohexamer; trimer of dimers Probable. Ref.3

Subcellular location

Cytoplasm Ref.3.

Induction

Transcription is repressed by glucose and by the binding of AraR to the operon promoter. L-arabinose acts as an inducer by inhibiting the binding of AraR to the DNA, thus allowing expression of the gene. Ref.2

Disruption phenotype

Cells lacking this gene retain 70% of arabinofuranosidase activity, and the double mutant abfA/abf2 is inactive. Ref.3

Sequence similarities

Belongs to the glycosyl hydrolase 51 family.

Biophysicochemical properties

Kinetic parameters:

KM=0.35 mM for sugar beet arabinan (branched) Ref.3

KM=0.42 mM for p-nitrophenyl-alpha-L-arabinofuranoside (pNP-Araf)

KM=0.5 mM for linear alpha-1,5-L-arabinan

KM=2.5 mM for arabinotriose

Vmax=311 µmol/min/mg enzyme with pNP-Araf as substrate

pH dependence:

Optimum pH is 8.

Temperature dependence:

Optimum temperature is 60 degrees Celsius.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
   Cellular componentCytoplasm
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processL-arabinose metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionalpha-N-arabinofuranosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 495495Intracellular exo-alpha-L-arabinofuranosidase 2
PRO_0000057702

Regions

Region171 – 1722Substrate binding By similarity

Sites

Active site1721Proton donor/acceptor By similarity
Active site2951Nucleophile By similarity
Binding site271Substrate By similarity
Binding site731Substrate; via amide nitrogen By similarity
Binding site941Substrate; via carbonyl oxygen By similarity
Binding site2121Substrate By similarity
Binding site2381Substrate By similarity
Binding site2951Substrate By similarity
Binding site3441Substrate By similarity
Site2991Important for substrate recognition By similarity
Site3441Important for substrate recognition By similarity

Amino acid modifications

Disulfide bond73 ↔ 176 By similarity

Experimental info

Sequence conflict441D → N in ABW70629. Ref.2
Sequence conflict631H → N in ABW70629. Ref.2
Sequence conflict1351S → A in ABW70629. Ref.2
Sequence conflict1651K → T in ABW70629. Ref.2
Sequence conflict203 – 2042DI → EL in ABW70629. Ref.2
Sequence conflict2171N → H in ABW70629. Ref.2
Sequence conflict2531E → D in ABW70629. Ref.2
Sequence conflict3401A → T in ABW70629. Ref.2
Sequence conflict3701N → E in ABW70629. Ref.2
Sequence conflict3821A → D in ABW70629. Ref.2
Sequence conflict3861M → T in ABW70629. Ref.2
Sequence conflict3931N → K in ABW70629. Ref.2
Sequence conflict4071Q → H in ABW70629. Ref.2
Sequence conflict4431V → I in ABW70629. Ref.2
Sequence conflict4481E → D in ABW70629. Ref.2
Sequence conflict4681R → S in ABW70629. Ref.2
Sequence conflict4731S → N in ABW70629. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P94552 [UniParc].

Last modified July 7, 2009. Version 2.
Checksum: 5D8F939DB55A6397

FASTA49556,475
        10         20         30         40         50         60 
MSEHQAVIQT DIAKGTINKN IYGHFAEHLG RGIYEGIWVG TDSDIPNING IRKDVLEALK 

        70         80         90        100        110        120 
QLHIPVLRWP GGCFADEYHW ANGVGDRKTM LNTHWGGTIE SNEFGTHEFM MLCELLECEP 

       130        140        150        160        170        180 
YICGNVGSGT VQEMSEWIEY MTFEEGTPMS DWRKQNGREE PWKLKYFGVG NENWGCGGNM 

       190        200        210        220        230        240 
HPEYYADLYR RFQTYVRNYS GNDIYKIAGG ANVDDFNWTD VLMKKAAGLM DGLSLHYYTI 

       250        260        270        280        290        300 
PGDFWKGKGS ATEFTEDEWF ITMKKAKYID ELIQKHGTIM DRYDPEQRVG LIIDEWGTWF 

       310        320        330        340        350        360 
DPEPGTNPGF LYQQNTIRDA LVAASHFHIF HQHCRRVQMA NIAQTVNVLQ AMILTEGERM 

       370        380        390        400        410        420 
LLTPTYHVFN MFKVHQDASL LATETMSADY EWNGETLPQI SISASKQAEG DINITICNID 

       430        440        450        460        470        480 
HQNKAEAEIE LRGLHKAADH SGVILTAEKM NAHNTFDDPH HVKPESFRQY TLSKNKLKVK 

       490 
LPPMSVVLLT LRADS

« Hide

References

« Hide 'large scale' references
[1]"The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism."
Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J., Emmerson P.T., Harwood C.R.
Microbiology 142:3067-3078(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"Transcriptional regulation of genes encoding arabinan-degrading enzymes in Bacillus subtilis."
Raposo M.P., Inacio J.M., Mota L.J., de Sa-Nogueira I.
J. Bacteriol. 186:1287-1296(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
Strain: 168.
[3]"Two distinct arabinofuranosidases contribute to arabino-oligosaccharide degradation in Bacillus subtilis."
Inacio J.M., Correia I.L., de Sa-Nogueira I.
Microbiology 154:2719-2729(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, DISRUPTION PHENOTYPE, NOMENCLATURE.
Strain: 168.
[4]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[5]"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 397.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z75208 Genomic DNA. Translation: CAA99576.1.
EU073712 Genomic DNA. Translation: ABW70629.1.
AL009126 Genomic DNA. Translation: CAB14811.2.
PIRG69734.
RefSeqNP_390729.2. NC_000964.3.

3D structure databases

ProteinModelPortalP94552.
SMRP94552. Positions 5-493.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU28510.

Protein family/group databases

CAZyGH51. Glycoside Hydrolase Family 51.

Proteomic databases

PaxDbP94552.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14811; CAB14811; BSU28510.
GeneID937449.
KEGGbsu:BSU28510.
PATRIC18977588. VBIBacSub10457_2982.

Organism-specific databases

GenoListBSU28510. [Micado]

Phylogenomic databases

eggNOGCOG3534.
HOGENOMHOG000236896.
KOK01209.
ProtClustDBCLSK2793876.

Enzyme and pathway databases

BioCycBSUB:BSU28510-MONOMER.
MetaCyc:BSU28510-MONOMER.
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. Glyco_hydro_cat. 1 hit.
ProtoNetSearch...

Entry information

Entry nameIABF2_BACSU
AccessionPrimary (citable) accession number: P94552
Secondary accession number(s): B5KLN7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 7, 2009
Last modified: May 1, 2013
This is version 81 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents