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Protein

Extracellular endo-alpha-(1->5)-L-arabinanase 1

Gene

abnA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the internal cleavage 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.3 Publications

Catalytic activityi

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

Cofactori

Ca2+CuratedNote: Binds 1 Ca2+ ion per subunit.Curated

Kineticsi

  1. KM=3.5 mM for arabinotetraose (at 27 degrees Celsius and pH 7)2 Publications
  2. KM=5.92 mM for linear 1,5-alpha-L-arabinan (at 37 degrees Celsius and pH 6.6)2 Publications
  1. Vmax=1.31 mmol/min/mg enzyme (at 37 degrees Celsius and pH 6.6)2 Publications

pH dependencei

Optimum pH is 6.0. At pH 4.0 the arabinosidase retains about 8% of activity.2 Publications

Temperature dependencei

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

Pathwayi: L-arabinan degradation

This protein is involved in the pathway L-arabinan degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway L-arabinan degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei44Proton acceptorBy similarity1
Binding sitei44SubstrateBy similarity1
Metal bindingi107CalciumSequence analysis1
Binding sitei125Substrate; via amide nitrogenBy similarity1
Sitei163Important for catalytic activity1
Metal bindingi165CalciumSequence analysis1
Active sitei215Proton donor1
Metal bindingi287CalciumSequence analysis1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BioCyciBSUB:BSU28810-MONOMER.
MetaCyc:BSU28810-MONOMER.
SABIO-RKP94522.
UniPathwayiUPA00667.

Protein family/group databases

CAZyiGH43. Glycoside Hydrolase Family 43.

Names & Taxonomyi

Protein namesi
Recommended name:
Extracellular endo-alpha-(1->5)-L-arabinanase 1 (EC:3.2.1.99)
Short name:
ABN
Alternative name(s):
Endo-1,5-alpha-L-arabinanase
Gene namesi
Name:abnA
Ordered Locus Names:BSU28810
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene retains about 40% of the capacity to hydrolyze linear arabinan compared to the wild-type.2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi43H → A: Decrease in binding affinity. 1 Publication1
Mutagenesisi44D → A: Loss of arabinanase activity. 1 Publication1
Mutagenesisi104W → A: Significantly less active (10000-fold) than the wild-type arabinanase against both linear arabinan and arabinooligosaccharides. 1 Publication1
Mutagenesisi124F → A: Increase in binding affinity. 1 Publication1
Mutagenesisi163D → A: Loss of arabinanase activity. 1 Publication1
Mutagenesisi181F → A: Significantly less active than the wild-type arabinanase against both linear arabinan (50-fold) and the arabinooligosaccharides (1000-fold). 1 Publication1
Mutagenesisi182W → A: Same binding affinity as wild-type. 1 Publication1
Mutagenesisi215E → A: Loss of arabinanase activity. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 321 PublicationAdd BLAST32
ChainiPRO_000036043733 – 323Extracellular endo-alpha-(1->5)-L-arabinanase 1Add BLAST291

Proteomic databases

PaxDbiP94522.

Expressioni

Inductioni

Induced by arabinose and arabina,n and repressed by glucose.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100015731.

Structurei

Secondary structure

1323
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi34 – 41Combined sources8
Beta strandi46 – 50Combined sources5
Beta strandi53 – 59Combined sources7
Beta strandi64 – 77Combined sources14
Beta strandi79 – 84Combined sources6
Helixi90 – 94Combined sources5
Beta strandi104 – 111Combined sources8
Beta strandi114 – 121Combined sources8
Beta strandi129 – 137Combined sources9
Turni139 – 142Combined sources4
Beta strandi145 – 153Combined sources9
Beta strandi157 – 159Combined sources3
Beta strandi165 – 168Combined sources4
Beta strandi174 – 178Combined sources5
Beta strandi185 – 190Combined sources6
Turni192 – 194Combined sources3
Beta strandi196 – 205Combined sources10
Turni208 – 212Combined sources5
Beta strandi214 – 222Combined sources9
Beta strandi225 – 233Combined sources9
Beta strandi235 – 239Combined sources5
Beta strandi242 – 252Combined sources11
Helixi265 – 267Combined sources3
Beta strandi271 – 274Combined sources4
Beta strandi278 – 289Combined sources12
Turni290 – 292Combined sources3
Beta strandi293 – 300Combined sources8
Turni301 – 305Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UV4X-ray1.50A31-307[»]
ProteinModelPortaliP94522.
SMRiP94522.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP94522.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni160 – 163Substrate bindingBy similarity4
Regioni180 – 182Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the glycosyl hydrolase 43 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4107PMW. Bacteria.
COG3507. LUCA.
HOGENOMiHOG000292006.
InParanoidiP94522.
KOiK06113.
OMAiYDANDNG.
PhylomeDBiP94522.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
InterProiIPR006710. Glyco_hydro_43.
IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PANTHERiPTHR22925. PTHR22925. 1 hit.
PfamiPF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
PIRSFiPIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
SUPFAMiSSF75005. SSF75005. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P94522-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKKKTWKRF LHFSSAALAA GLIFTSAAPA EAAFWGASNE LLHDPTMIKE
60 70 80 90 100
GSSWYALGTG LTEERGLRVL KSSDAKNWTV QKSIFTTPLS WWSNYVPNYG
110 120 130 140 150
QNQWAPDIQY YNGKYWLYYS VSSFGSNTSA IGLASSTSIS SGGWKDEGLV
160 170 180 190 200
IRSTSSNNYN AIDPELTFDK DGNPWLAFGS FWSGIKLTKL DKSTMKPTGS
210 220 230 240 250
LYSIAARPNN GGALEAPTLT YQNGYYYLMV SFDKCCDGVN STYKIAYGRS
260 270 280 290 300
KSITGPYLDK SGKSMLEGGG TILDSGNDQW KGPGGQDIVN GNILVRHAYD
310 320
ANDNGIPKLL INDLNWSSGW PSY
Length:323
Mass (Da):35,446
Last modified:July 7, 2009 - v3
Checksum:i0105FB280E83BC69
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti172G → D in CAA99586 (PubMed:8969504).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75208 Genomic DNA. Translation: CAA99586.1. Frameshift.
AY669857 Genomic DNA. Translation: AAV87172.1.
AL009126 Genomic DNA. Translation: CAB14841.2.
PIRiE69580.
RefSeqiNP_390759.2. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB14841; CAB14841; BSU28810.
GeneIDi937430.
KEGGibsu:BSU28810.
PATRICi18977654. VBIBacSub10457_3015.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75208 Genomic DNA. Translation: CAA99586.1. Frameshift.
AY669857 Genomic DNA. Translation: AAV87172.1.
AL009126 Genomic DNA. Translation: CAB14841.2.
PIRiE69580.
RefSeqiNP_390759.2. NC_000964.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UV4X-ray1.50A31-307[»]
ProteinModelPortaliP94522.
SMRiP94522.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100015731.

Protein family/group databases

CAZyiGH43. Glycoside Hydrolase Family 43.

Proteomic databases

PaxDbiP94522.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14841; CAB14841; BSU28810.
GeneIDi937430.
KEGGibsu:BSU28810.
PATRICi18977654. VBIBacSub10457_3015.

Phylogenomic databases

eggNOGiENOG4107PMW. Bacteria.
COG3507. LUCA.
HOGENOMiHOG000292006.
InParanoidiP94522.
KOiK06113.
OMAiYDANDNG.
PhylomeDBiP94522.

Enzyme and pathway databases

UniPathwayiUPA00667.
BioCyciBSUB:BSU28810-MONOMER.
MetaCyc:BSU28810-MONOMER.
SABIO-RKP94522.

Miscellaneous databases

EvolutionaryTraceiP94522.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
InterProiIPR006710. Glyco_hydro_43.
IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PANTHERiPTHR22925. PTHR22925. 1 hit.
PfamiPF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
PIRSFiPIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
SUPFAMiSSF75005. SSF75005. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiEABN1_BACSU
AccessioniPrimary (citable) accession number: P94522
Secondary accession number(s): Q5MPF4, Q795W7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: July 7, 2009
Last modified: November 2, 2016
This is version 101 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.