Skip Header

Contribute Send feedback
Read comments (?) or add your own

P94522 (ABNA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | 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:
Arabinan endo-1,5-alpha-L-arabinosidase
EC=3.2.1.99
Alternative name(s):
Endo-1,5-alpha-L-arabinanase
Short name=ABN
Endo-arabinanase
Gene names
Name:abnA
Ordered Locus Names:BSU28810
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length323 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the hydrolysis of the alpha-1,5-linked L-arabinofuranoside backbone. Its preferred substrate is linear 1,5-alpha-L-arabinan. It is also active towards branched sugar beet arabinan, but inactive towards larch wood arabinogalactan, wheat arabinoxylan and p-nitrophenyl-alpha-L-arabinofuranoside. The enzyme activity is progressively reduced as 1,5-alpha-chains become shorter or more highly substituted. Ref.5

Catalytic activity

Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.

Pathway

Glycan metabolism; L-arabinan degradation.

Subcellular location

Secreted Potential Ref.2.

Induction

Induced by arabinose and arabinan and repressed by glucose. Ref.5

Sequence similarities

Belongs to the glycosyl hydrolase 43 family.

Biophysicochemical properties

Kinetic parameters:

KM=3.5 mM for arabinotetraose (at 27 degrees Celsius and pH 7) Ref.6

KM=5.92 mM for linear 1,5-alpha-L-arabinan (at 37 degrees Celsius and pH 6.6)

Vmax=1.31 mmol/min/mg enzyme (at 37 degrees Celsius and pH 6.6)

pH dependence:

Optimum pH is 6.0. At pH 4.0 the arabinosidase retains about 8% of activity.

Temperature dependence:

Optimum temperature is 60 degrees Celsius. At 80 degrees Celsius retains about 2% of activity.

Sequence caution

The sequence CAA99586.1 differs from that shown. Reason: Frameshift at position 308.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionarabinan endo-1,5-alpha-L-arabinosidase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3232 Potential
Chain33 – 323291Arabinan endo-1,5-alpha-L-arabinosidase
PRO_0000360437

Experimental info

Mutagenesis431H → A: Decrease in binding affinity. Ref.6
Mutagenesis441D → A: Loss of arabinosidase activity. Ref.6
Mutagenesis1041W → A: Significantly less active (10000-fold) than the wild-type arabinosidase against both linear arabinan and arabinooligosaccharides. Ref.6
Mutagenesis1241F → A: Increase in binding affinity. Ref.6
Mutagenesis1631D → A: Loss of arabinosidase activity. Ref.6
Mutagenesis1811F → A: Significantly less active than the wild-type arabinosidase against both linear arabinan (50-fold) and the arabinooligosaccharides (1000-fold). Ref.6
Mutagenesis1821W → A: Same binding affinity as wild-type. Ref.6
Mutagenesis2151E → A: Loss of arabinosidase activity. Ref.2 Ref.6
Sequence conflict1721G → D in CAA99586. Ref.1

Secondary structure

1 ......................................................... 323
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P94522 [UniParc].

Last modified July 7, 2009. Version 3.
Checksum: 0105FB280E83BC69

FASTA32335,446
        10         20         30         40         50         60 
MKKKKTWKRF LHFSSAALAA GLIFTSAAPA EAAFWGASNE LLHDPTMIKE GSSWYALGTG 

        70         80         90        100        110        120 
LTEERGLRVL KSSDAKNWTV QKSIFTTPLS WWSNYVPNYG QNQWAPDIQY YNGKYWLYYS 

       130        140        150        160        170        180 
VSSFGSNTSA IGLASSTSIS SGGWKDEGLV IRSTSSNNYN AIDPELTFDK DGNPWLAFGS 

       190        200        210        220        230        240 
FWSGIKLTKL DKSTMKPTGS LYSIAARPNN GGALEAPTLT YQNGYYYLMV SFDKCCDGVN 

       250        260        270        280        290        300 
STYKIAYGRS KSITGPYLDK SGKSMLEGGG TILDSGNDQW KGPGGQDIVN GNILVRHAYD 

       310        320 
ANDNGIPKLL INDLNWSSGW PSY

« 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: 8969504] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"Purification, characterization and functional analysis of an endo-arabinanase (AbnA) from Bacillus subtilis."
Leal T.F., de Sa-Nogueira I.
FEMS Microbiol. Lett. 241:41-48(2004) [PubMed: 15556708] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 33-37, SUBCELLULAR LOCATION, MUTAGENESIS OF GLU-215.
Strain: 168.
[3]"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: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"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: 19383706] [Abstract]
Cited for: SEQUENCE REVISION TO 172 AND C-TERMINUS.
[5]"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: 14973026] [Abstract]
Cited for: FUNCTION, INDUCTION.
Strain: 168.
[6]"Tailored catalysts for plant cell-wall degradation: redesigning the exo/endo preference of Cellvibrio japonicus arabinanase 43A."
Proctor M.R., Taylor E.J., Nurizzo D., Turkenburg J.P., Lloyd R.M., Vardakou M., Davies G.J., Gilbert H.J.
Proc. Natl. Acad. Sci. U.S.A. 102:2697-2702(2005) [PubMed: 15708971] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 31-323, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-43; ASP-44; TRP-104; PHE-124; ASP-163; PHE-181; TRP-182 AND GLU-215.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Z75208 Genomic DNA. Translation: CAA99586.1. Frameshift.
AY669857 Genomic DNA. Translation: AAV87172.1.
AL009126 Genomic DNA. Translation: CAB14841.2.
PIRE69580.
RefSeqNP_390759.2. NC_000964.3.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UV4X-ray1.50A31-323[»]
ProteinModelPortalP94522.
SMRP94522. Positions 33-323.
ModBaseSearch...

Protein family/group databases

CAZyGH43. Glycoside Hydrolase Family 43.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000001491; EBBACP00000001491; EBBACG00000001489.
GeneID937430.
GenomeReviewsGene locus BSU28810 in contig AL009126_GR.
KEGGbsu:BSU28810.
NMPDRfig|224308.1.peg.2884.
PATRIC18977654. VBIBacSub10457_3015.

Organism-specific databases

GenoListBSU28810. [Micado]

Phylogenomic databases

GeneTreeEBGT00050000001042.
HOGENOMHBG346382.
PhylomeDBP94522.
ProtClustDBCLSK887698.

Enzyme and pathway databases

BioCycBSUB:BSU28810-MONOMER.
MetaCyc:BSU28810-MONOMER.

Family and domain databases

InterProIPR006710. Glyco_hydro_43.
IPR023296. Glyco_hydro_43_beta-prop.
IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
[Graphical view]
Gene3DG3DSA:2.115.10.20. Glyco_hydro_43_beta-prop. 1 hit.
KOK06113.
PANTHERPTHR22925. Glyco_hydro_43. 1 hit.
PfamPF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
PIRSFPIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
SUPFAMSSF75005. Glyco_hydro_43_beta-prop. 1 hit.
ProtoNetSearch...

Entry information

Entry nameABNA_BACSU
AccessionPrimary (citable) accession number: P94522
Secondary accession number(s): Q5MPF4, Q795W7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: July 7, 2009
Last modified: January 25, 2012
This is version 69 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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