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P94531

- IABF1_BACSU

UniProt

P94531 - IABF1_BACSU

Protein

Intracellular exo-alpha-(1->5)-L-arabinofuranosidase 1

Gene

abfA

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 93 (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-(1->5)-arabinofuranosyl bonds in different hemicellulosic homopolysaccharides (branched and debranched arabinans). It acts preferentially on arabinotriose, arabinobiose and linear alpha-(1->5)-L-arabinan, and is much less effective on branched sugar beet arabinan.1 Publication

    Catalytic activityi

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

    Kineticsi

    1. KM=0.36 mM for linear alpha-1,5-L-arabinan (at pH 6.6 and 37 degrees Celsius)1 Publication
    2. KM=0.49 mM for p-nitrophenyl-alpha-L-arabinofuranoside (pNP-Araf) (at pH 6.6 and 37 degrees Celsius)1 Publication
    3. KM=0.78 mM for arabinobiose (at pH 6.6 and 37 degrees Celsius)1 Publication
    4. KM=1.1 mM for arabinotriose (at pH 6.6 and 37 degrees Celsius)1 Publication
    5. KM=4.4 mM for sugar beet arabinan (branched) (at pH 6.6 and 37 degrees Celsius)1 Publication

    Vmax=317 µmol/min/mg enzyme with pNP-Araf as substrate (at pH 6.6 and 37 degrees Celsius)1 Publication

    pH dependencei

    Optimum pH is 8.1 Publication

    Temperature dependencei

    Optimum temperature is 50 degrees Celsius.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei27 – 271SubstrateBy similarity
    Binding sitei72 – 721Substrate; via amide nitrogenBy similarity
    Active sitei173 – 1731Proton donor/acceptorBy similarity
    Binding sitei244 – 2441SubstrateBy similarity
    Active sitei292 – 2921NucleophileBy similarity
    Binding sitei292 – 2921SubstrateBy similarity
    Sitei296 – 2961Important for substrate recognitionBy similarity
    Binding sitei349 – 3491SubstrateBy similarity
    Sitei349 – 3491Important 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:BSU28720-MONOMER.
    MetaCyc:BSU28720-MONOMER.
    SABIO-RKP94531.
    UniPathwayiUPA00667.

    Protein family/group databases

    CAZyiGH51. Glycoside Hydrolase Family 51.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Intracellular exo-alpha-(1->5)-L-arabinofuranosidase 1 (EC:3.2.1.55)
    Short name:
    ABF
    Alternative name(s):
    Intracellular arabinan exo-alpha-(1->5)-L-arabinosidase
    Short name:
    Arabinosidase
    Gene namesi
    Name:abfA
    Ordered Locus Names:BSU28720
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU28720. [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 38% of arabinofuranosidase activity, and the double mutant abfA/abf2 is inactive.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 500500Intracellular exo-alpha-(1->5)-L-arabinofuranosidase 1PRO_0000057701Add
    BLAST

    Proteomic databases

    PaxDbiP94531.

    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 Probable.2 Publications

    Interactioni

    Subunit structurei

    Homohexamer; trimer of dimers.1 Publication

    Protein-protein interaction databases

    STRINGi224308.BSU28720.

    Structurei

    3D structure databases

    ProteinModelPortaliP94531.
    SMRiP94531. Positions 3-498.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni172 – 1732Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 51 family.Curated

    Phylogenomic databases

    eggNOGiCOG3534.
    HOGENOMiHOG000236895.
    KOiK01209.
    OrthoDBiEOG6SJJF9.
    PhylomeDBiP94531.

    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.

    P94531-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKARMIVDK EYKIGEVDKR IYGSFIEHMG RAVYEGIYEP DHPEADEDGF    50
    RKDVQSLIKE LQVPIIRYPG GNFLSGYNWE DGVGPVENRP RRLDLAWQTT 100
    ETNEVGTNEF LSWAKKVNTE VNMAVNLGTR GIDAARNLVE YCNHPKGSYW 150
    SDLRRSHGYE QPYGIKTWCL GNEMDGPWQI GHKTADEYGR LAAETAKVMK 200
    WVDPSIELVA CGSSNSGMPT FIDWEAKVLE HTYEHVDYIS LHTYYGNRDN 250
    NLPNYLARSM DLDHFIKSVA ATCDYVKAKT RSKKTINLSL DEWNVWYHSN 300
    EADKKVEPWI TARPILEDIY NFEDALLVGS LLITMLQHAD RVKIACLAQL 350
    VNVIAPIMTE KGGEAWRQPI FYPYMHASVY GRGESLKPLI SSPKYDCSDF 400
    TDVPYVDAAV VYSEEEETLT IFAVNKAEDQ METEISLRGF ESYQIAEHIV 450
    LEHQDIKATN QHNRKNVVPH SNGSSSVSEN GLTAHFTPLS WNVIRLKKQS 500
    Length:500
    Mass (Da):57,034
    Last modified:July 7, 2009 - v2
    Checksum:i3EEA8F8ADA3D705A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti114 – 1141A → P in CAA99595. (PubMed:8969504)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89810 Genomic DNA. Translation: CAA61937.1.
    Z75208 Genomic DNA. Translation: CAA99595.1.
    AL009126 Genomic DNA. Translation: CAB14832.2.
    PIRiC69580.
    RefSeqiNP_390750.2. NC_000964.3.

    Genome annotation databases

    EnsemblBacteriaiCAB14832; CAB14832; BSU28720.
    GeneIDi937509.
    KEGGibsu:BSU28720.
    PATRICi18977636. VBIBacSub10457_3006.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X89810 Genomic DNA. Translation: CAA61937.1 .
    Z75208 Genomic DNA. Translation: CAA99595.1 .
    AL009126 Genomic DNA. Translation: CAB14832.2 .
    PIRi C69580.
    RefSeqi NP_390750.2. NC_000964.3.

    3D structure databases

    ProteinModelPortali P94531.
    SMRi P94531. Positions 3-498.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU28720.

    Protein family/group databases

    CAZyi GH51. Glycoside Hydrolase Family 51.

    Proteomic databases

    PaxDbi P94531.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB14832 ; CAB14832 ; BSU28720 .
    GeneIDi 937509.
    KEGGi bsu:BSU28720.
    PATRICi 18977636. VBIBacSub10457_3006.

    Organism-specific databases

    GenoListi BSU28720. [Micado ]

    Phylogenomic databases

    eggNOGi COG3534.
    HOGENOMi HOG000236895.
    KOi K01209.
    OrthoDBi EOG6SJJF9.
    PhylomeDBi P94531.

    Enzyme and pathway databases

    UniPathwayi UPA00667 .
    BioCyci BSUB:BSU28720-MONOMER.
    MetaCyc:BSU28720-MONOMER.
    SABIO-RK P94531.

    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 Bacillus subtilis L-arabinose (ara) operon: nucleotide sequence, genetic organization and expression."
      Sa-Nogueira I.M.G., Nogueira T.V., Soares S., de Lencastre H.
      Microbiology 143:957-969(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "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.
    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.
      , 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 114.
    5. "Mode of action of AraR, the key regulator of L-arabinose metabolism in Bacillus subtilis."
      Mota L.J., Tavares P., Sa-Nogueira I.M.G.
      Mol. Microbiol. 33:476-489(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TRANSCRIPTIONAL REGULATION.
    6. "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: INDUCTION.
      Strain: 168.
    7. "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: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, DISRUPTION PHENOTYPE, SUBUNIT.

    Entry informationi

    Entry nameiIABF1_BACSU
    AccessioniPrimary (citable) accession number: P94531
    Secondary accession number(s): O05096
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 7, 2009
    Last modified: October 1, 2014
    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