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P94552

- IABF2_BACSU

UniProt

P94552 - IABF2_BACSU

Protein

Intracellular exo-alpha-L-arabinofuranosidase 2

Gene

abf2

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (07 Jul 2009)
      Previous versions | rss
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    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

    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

    Pathwayi

    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

    1. alpha-L-arabinofuranosidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. arabinan catabolic process Source: UniProtKB-UniPathway
    2. L-arabinose metabolic process Source: InterPro

    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: Chromosome

    Organism-specific databases

    GenoListiBSU28510. [Micado]

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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.BSU28510.

    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.
    KOiK01209.
    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

    MSEHQAVIQT DIAKGTINKN IYGHFAEHLG RGIYEGIWVG TDSDIPNING    50
    IRKDVLEALK QLHIPVLRWP GGCFADEYHW ANGVGDRKTM LNTHWGGTIE 100
    SNEFGTHEFM MLCELLECEP YICGNVGSGT VQEMSEWIEY MTFEEGTPMS 150
    DWRKQNGREE PWKLKYFGVG NENWGCGGNM HPEYYADLYR RFQTYVRNYS 200
    GNDIYKIAGG ANVDDFNWTD VLMKKAAGLM DGLSLHYYTI PGDFWKGKGS 250
    ATEFTEDEWF ITMKKAKYID ELIQKHGTIM DRYDPEQRVG LIIDEWGTWF 300
    DPEPGTNPGF LYQQNTIRDA LVAASHFHIF HQHCRRVQMA NIAQTVNVLQ 350
    AMILTEGERM LLTPTYHVFN MFKVHQDASL LATETMSADY EWNGETLPQI 400
    SISASKQAEG DINITICNID HQNKAEAEIE LRGLHKAADH SGVILTAEKM 450
    NAHNTFDDPH HVKPESFRQY TLSKNKLKVK LPPMSVVLLT LRADS 495
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z75208 Genomic DNA. Translation: CAA99576.1 .
    EU073712 Genomic DNA. Translation: ABW70629.1 .
    AL009126 Genomic DNA. Translation: CAB14811.2 .
    PIRi G69734.
    RefSeqi NP_390729.2. NC_000964.3.

    3D structure databases

    ProteinModelPortali P94552.
    SMRi P94552. Positions 5-493.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU28510.

    Protein family/group databases

    CAZyi GH51. Glycoside Hydrolase Family 51.

    Proteomic databases

    PaxDbi P94552.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB14811 ; CAB14811 ; BSU28510 .
    GeneIDi 937449.
    KEGGi bsu:BSU28510.
    PATRICi 18977588. VBIBacSub10457_2982.

    Organism-specific databases

    GenoListi BSU28510. [Micado ]

    Phylogenomic databases

    eggNOGi COG3534.
    HOGENOMi HOG000236896.
    KOi K01209.
    OrthoDBi EOG6HF5XV.
    PhylomeDBi P94552.

    Enzyme and pathway databases

    UniPathwayi UPA00667 .
    BioCyci BSUB:BSU28510-MONOMER.
    MetaCyc:BSU28510-MONOMER.
    SABIO-RK P94552.

    Family and domain databases

    Gene3Di 3.20.20.80. 1 hit.
    InterProi IPR010720. Alpha-L-AF_C.
    IPR013781. Glyco_hydro_catalytic_dom.
    IPR017853. Glycoside_hydrolase_SF.
    [Graphical view ]
    Pfami PF06964. Alpha-L-AF_C. 1 hit.
    [Graphical view ]
    SMARTi SM00813. Alpha-L-AF_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51445. SSF51445. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 89 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