Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Intracellular exo-alpha-L-arabinofuranosidase 2

Gene

abf2

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 cleavage 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.1 Publication

Catalytic activityi

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

Kineticsi

  1. KM=0.35 mM for sugar beet arabinan (branched)1 Publication
  2. KM=0.42 mM for p-nitrophenyl-alpha-L-arabinofuranoside (pNP-Araf)1 Publication
  3. KM=0.5 mM for linear alpha-1,5-L-arabinan1 Publication
  4. KM=2.5 mM for arabinotriose1 Publication
  1. Vmax=311 µmol/min/mg enzyme with pNP-Araf as substrate1 Publication

pH dependencei

Optimum pH is 8.1 Publication

Temperature dependencei

Optimum temperature is 60 degrees Celsius.1 Publication

Pathway:iL-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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei27 – 271SubstrateBy similarity
Binding sitei73 – 731Substrate; via amide nitrogenBy similarity
Binding sitei94 – 941Substrate; via carbonyl oxygenBy similarity
Active sitei172 – 1721Proton donor/acceptorBy similarity
Binding sitei212 – 2121SubstrateBy similarity
Binding sitei238 – 2381SubstrateBy similarity
Active sitei295 – 2951NucleophileBy similarity
Binding sitei295 – 2951SubstrateBy similarity
Sitei299 – 2991Important for substrate recognitionBy similarity
Binding sitei344 – 3441SubstrateBy similarity
Sitei344 – 3441Important for substrate recognitionBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism

Enzyme and pathway databases

BioCyciBSUB:BSU28510-MONOMER.
MetaCyc:BSU28510-MONOMER.
SABIO-RKP94552.
UniPathwayiUPA00667.

Protein family/group databases

CAZyiGH51. Glycoside Hydrolase Family 51.

Names & Taxonomyi

Protein namesi
Recommended name:
Intracellular exo-alpha-L-arabinofuranosidase 2 (EC:3.2.1.55)
Short name:
ABF
Alternative name(s):
Intracellular arabinan exo-alpha-L-arabinosidase
Short name:
Arabinosidase
Gene namesi
Name:abf2
Synonyms:asd, xsa
Ordered Locus Names:BSU28510
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570 Componenti: Chromosome

Organism-specific databases

GenoListiBSU28510. [Micado]

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene retain 70% of arabinofuranosidase activity, and the double mutant abfA/abf2 is inactive.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 495495Intracellular exo-alpha-L-arabinofuranosidase 2PRO_0000057702Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi73 ↔ 176By similarity

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiP94552.

Expressioni

Inductioni

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.1 Publication

Interactioni

Subunit structurei

Homohexamer; trimer of dimers.1 Publication

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100015566.

Structurei

3D structure databases

ProteinModelPortaliP94552.
SMRiP94552. Positions 5-493.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni171 – 1722Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the glycosyl hydrolase 51 family.Curated

Phylogenomic databases

eggNOGiCOG3534.
HOGENOMiHOG000236896.
InParanoidiP94552.
KOiK01209.
OMAiRMVNTHW.
OrthoDBiEOG6HF5XV.
PhylomeDBiP94552.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR010720. Alpha-L-AF_C.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF06964. Alpha-L-AF_C. 1 hit.
[Graphical view]
SMARTiSM00813. Alpha-L-AF_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

P94552-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEHQAVIQT DIAKGTINKN IYGHFAEHLG RGIYEGIWVG TDSDIPNING
60 70 80 90 100
IRKDVLEALK QLHIPVLRWP GGCFADEYHW ANGVGDRKTM LNTHWGGTIE
110 120 130 140 150
SNEFGTHEFM MLCELLECEP YICGNVGSGT VQEMSEWIEY MTFEEGTPMS
160 170 180 190 200
DWRKQNGREE PWKLKYFGVG NENWGCGGNM HPEYYADLYR RFQTYVRNYS
210 220 230 240 250
GNDIYKIAGG ANVDDFNWTD VLMKKAAGLM DGLSLHYYTI PGDFWKGKGS
260 270 280 290 300
ATEFTEDEWF ITMKKAKYID ELIQKHGTIM DRYDPEQRVG LIIDEWGTWF
310 320 330 340 350
DPEPGTNPGF LYQQNTIRDA LVAASHFHIF HQHCRRVQMA NIAQTVNVLQ
360 370 380 390 400
AMILTEGERM LLTPTYHVFN MFKVHQDASL LATETMSADY EWNGETLPQI
410 420 430 440 450
SISASKQAEG DINITICNID HQNKAEAEIE LRGLHKAADH SGVILTAEKM
460 470 480 490
NAHNTFDDPH HVKPESFRQY TLSKNKLKVK LPPMSVVLLT LRADS
Length:495
Mass (Da):56,475
Last modified:July 7, 2009 - v2
Checksum:i5D8F939DB55A6397
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441D → N in ABW70629 (PubMed:14973026).Curated
Sequence conflicti63 – 631H → N in ABW70629 (PubMed:14973026).Curated
Sequence conflicti135 – 1351S → A in ABW70629 (PubMed:14973026).Curated
Sequence conflicti165 – 1651K → T in ABW70629 (PubMed:14973026).Curated
Sequence conflicti203 – 2042DI → EL in ABW70629 (PubMed:14973026).Curated
Sequence conflicti217 – 2171N → H in ABW70629 (PubMed:14973026).Curated
Sequence conflicti253 – 2531E → D in ABW70629 (PubMed:14973026).Curated
Sequence conflicti340 – 3401A → T in ABW70629 (PubMed:14973026).Curated
Sequence conflicti370 – 3701N → E in ABW70629 (PubMed:14973026).Curated
Sequence conflicti382 – 3821A → D in ABW70629 (PubMed:14973026).Curated
Sequence conflicti386 – 3861M → T in ABW70629 (PubMed:14973026).Curated
Sequence conflicti393 – 3931N → K in ABW70629 (PubMed:14973026).Curated
Sequence conflicti407 – 4071Q → H in ABW70629 (PubMed:14973026).Curated
Sequence conflicti443 – 4431V → I in ABW70629 (PubMed:14973026).Curated
Sequence conflicti448 – 4481E → D in ABW70629 (PubMed:14973026).Curated
Sequence conflicti468 – 4681R → S in ABW70629 (PubMed:14973026).Curated
Sequence conflicti473 – 4731S → N in ABW70629 (PubMed:14973026).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75208 Genomic DNA. Translation: CAA99576.1.
EU073712 Genomic DNA. Translation: ABW70629.1.
AL009126 Genomic DNA. Translation: CAB14811.2.
PIRiG69734.
RefSeqiNP_390729.2. NC_000964.3.
WP_004398654.1. NZ_JNCM01000036.1.

Genome annotation databases

EnsemblBacteriaiCAB14811; CAB14811; BSU28510.
GeneIDi937449.
KEGGibsu:BSU28510.
PATRICi18977588. VBIBacSub10457_2982.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z75208 Genomic DNA. Translation: CAA99576.1.
EU073712 Genomic DNA. Translation: ABW70629.1.
AL009126 Genomic DNA. Translation: CAB14811.2.
PIRiG69734.
RefSeqiNP_390729.2. NC_000964.3.
WP_004398654.1. NZ_JNCM01000036.1.

3D structure databases

ProteinModelPortaliP94552.
SMRiP94552. Positions 5-493.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100015566.

Protein family/group databases

CAZyiGH51. Glycoside Hydrolase Family 51.

Proteomic databases

PaxDbiP94552.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB14811; CAB14811; BSU28510.
GeneIDi937449.
KEGGibsu:BSU28510.
PATRICi18977588. VBIBacSub10457_2982.

Organism-specific databases

GenoListiBSU28510. [Micado]

Phylogenomic databases

eggNOGiCOG3534.
HOGENOMiHOG000236896.
InParanoidiP94552.
KOiK01209.
OMAiRMVNTHW.
OrthoDBiEOG6HF5XV.
PhylomeDBiP94552.

Enzyme and pathway databases

UniPathwayiUPA00667.
BioCyciBSUB:BSU28510-MONOMER.
MetaCyc:BSU28510-MONOMER.
SABIO-RKP94552.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR010720. Alpha-L-AF_C.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF06964. Alpha-L-AF_C. 1 hit.
[Graphical view]
SMARTiSM00813. Alpha-L-AF_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiIABF2_BACSU
AccessioniPrimary (citable) accession number: P94552
Secondary accession number(s): B5KLN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 7, 2009
Last modified: June 24, 2015
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.