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P94522 (EABN1_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 80. 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:
Extracellular endo-alpha-(1->5)-L-arabinanase 1
Short name=ABN
EC=3.2.1.99
Alternative name(s):
Endo-1,5-alpha-L-arabinanase
Gene names
Name:abnA
Ordered Locus Names:BSU28810
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › 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

Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleveage of alpha-(1->5)-L-arabinofuranosyl residues of linear 1,5-alpha-L-arabinan and of branched sugar beet arabinan. It displays no activity against heavily substituted arabinans or a range of other polysaccharides (larch wood arabinogalactan, wheat arabinoxylan and p-nitrophenyl-alpha-L-arabinofuranoside). The enzyme activity is progressively reduced as alpha-(1->5)-chains become shorter or more highly substituted. Ref.2 Ref.5 Ref.6

Catalytic activity

Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans. Ref.2

Cofactor

Binds 1 calcium ion per subunit Potential. Ref.6

Pathway

Glycan metabolism; L-arabinan degradation.

Subcellular location

Secreted Ref.2.

Induction

Induced by arabinose and arabina,n and repressed by glucose. Ref.5

Disruption phenotype

Cells lacking this gene retains about 40% of the capacity to hydrolyze linear arabinan compared to the wild-type. Ref.2 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.2 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
   Biological processCarbohydrate metabolism
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processarabinan catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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 Ref.2
Chain33 – 323291Extracellular endo-alpha-(1->5)-L-arabinanase 1
PRO_0000360437

Regions

Region160 – 1634Substrate binding By similarity
Region180 – 1823Substrate binding By similarity

Sites

Active site441Proton acceptor By similarity
Active site2151Proton donor
Metal binding1071Calcium ion Potential
Metal binding1651Calcium ion Potential
Metal binding2871Calcium ion Potential
Binding site441Substrate By similarity
Binding site1251Substrate; via amide nitrogen By similarity
Site1631Important for catalytic activity

Experimental info

Mutagenesis431H → A: Decrease in binding affinity. Ref.6
Mutagenesis441D → A: Loss of arabinanase activity. Ref.6
Mutagenesis1041W → A: Significantly less active (10000-fold) than the wild-type arabinanase against both linear arabinan and arabinooligosaccharides. Ref.6
Mutagenesis1241F → A: Increase in binding affinity. Ref.6
Mutagenesis1631D → A: Loss of arabinanase activity. Ref.6
Mutagenesis1811F → A: Significantly less active than the wild-type arabinanase 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 arabinanase 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 33-37, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-215, DISRUPTION PHENOTYPE, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, SUBSTRATE SPECIFICITY.
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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, 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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 31-323 IN COMPLEX WITH CALCIUM IONS, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF HIS-43; ASP-44; TRP-104; PHE-124; ASP-163; PHE-181; TRP-182 AND GLU-215, COFACTOR, SUBSTRATE SPECIFICITY.

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-protein interaction databases

STRING224308.BSU28810.

Protein family/group databases

CAZyGH43. Glycoside Hydrolase Family 43.

Proteomic databases

PaxDbP94522.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14841; CAB14841; BSU28810.
GeneID937430.
KEGGbsu:BSU28810.
PATRIC18977654. VBIBacSub10457_3015.

Organism-specific databases

GenoListBSU28810. [Micado]

Phylogenomic databases

eggNOGCOG3507.
HOGENOMHOG000292006.
KOK06113.
ProtClustDBCLSK887698.

Enzyme and pathway databases

BioCycBSUB:BSU28810-MONOMER.
MetaCyc:BSU28810-MONOMER.
UniPathwayUPA00667.

Family and domain databases

Gene3D2.115.10.20. 1 hit.
InterProIPR006710. Glyco_hydro_43.
IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PANTHERPTHR22925. PTHR22925. 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...

Other

EvolutionaryTraceP94522.

Entry information

Entry nameEABN1_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: May 1, 2013
This is version 80 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