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P94522

- EABN1_BACSU

UniProt

P94522 - EABN1_BACSU

Protein

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

Gene

abnA

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 88 (01 Oct 2014)
      Sequence version 3 (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 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

    Binds 1 calcium 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

    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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei44 – 441Proton acceptorBy similarity
    Binding sitei44 – 441SubstrateBy similarity
    Metal bindingi107 – 1071Calcium ionSequence Analysis
    Binding sitei125 – 1251Substrate; via amide nitrogenBy similarity
    Sitei163 – 1631Important for catalytic activity
    Metal bindingi165 – 1651Calcium ionSequence Analysis
    Active sitei215 – 2151Proton donor
    Metal bindingi287 – 2871Calcium ionSequence Analysis

    GO - Molecular functioni

    1. arabinan endo-1,5-alpha-L-arabinosidase activity Source: UniProtKB-EC
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. arabinan catabolic process Source: UniProtKB-UniPathway

    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
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU28810. [Micado]

    Subcellular locationi

    Secreted 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    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)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi43 – 431H → A: Decrease in binding affinity. 1 Publication
    Mutagenesisi44 – 441D → A: Loss of arabinanase activity. 1 Publication
    Mutagenesisi104 – 1041W → A: Significantly less active (10000-fold) than the wild-type arabinanase against both linear arabinan and arabinooligosaccharides. 1 Publication
    Mutagenesisi124 – 1241F → A: Increase in binding affinity. 1 Publication
    Mutagenesisi163 – 1631D → A: Loss of arabinanase activity. 1 Publication
    Mutagenesisi181 – 1811F → A: Significantly less active than the wild-type arabinanase against both linear arabinan (50-fold) and the arabinooligosaccharides (1000-fold). 1 Publication
    Mutagenesisi182 – 1821W → A: Same binding affinity as wild-type. 1 Publication
    Mutagenesisi215 – 2151E → A: Loss of arabinanase activity. 2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 32321 PublicationAdd
    BLAST
    Chaini33 – 323291Extracellular endo-alpha-(1->5)-L-arabinanase 1PRO_0000360437Add
    BLAST

    Proteomic databases

    PaxDbiP94522.

    Expressioni

    Inductioni

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

    Interactioni

    Protein-protein interaction databases

    STRINGi224308.BSU28810.

    Structurei

    Secondary structure

    1
    323
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi34 – 418
    Beta strandi46 – 505
    Beta strandi53 – 597
    Beta strandi64 – 7714
    Beta strandi79 – 846
    Helixi90 – 945
    Beta strandi104 – 1118
    Beta strandi114 – 1218
    Beta strandi129 – 1379
    Turni139 – 1424
    Beta strandi145 – 1539
    Beta strandi157 – 1593
    Beta strandi165 – 1684
    Beta strandi174 – 1785
    Beta strandi185 – 1906
    Turni192 – 1943
    Beta strandi196 – 20510
    Turni208 – 2125
    Beta strandi214 – 2229
    Beta strandi225 – 2339
    Beta strandi235 – 2395
    Beta strandi242 – 25211
    Helixi265 – 2673
    Beta strandi271 – 2744
    Beta strandi278 – 28912
    Turni290 – 2923
    Beta strandi293 – 3008
    Turni301 – 3055

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UV4X-ray1.50A31-307[»]
    ProteinModelPortaliP94522.
    SMRiP94522. Positions 33-323.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP94522.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni160 – 1634Substrate bindingBy similarity
    Regioni180 – 1823Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 43 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiCOG3507.
    HOGENOMiHOG000292006.
    KOiK06113.
    OrthoDBiEOG686NDH.
    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

    MKKKKTWKRF LHFSSAALAA GLIFTSAAPA EAAFWGASNE LLHDPTMIKE    50
    GSSWYALGTG LTEERGLRVL KSSDAKNWTV QKSIFTTPLS WWSNYVPNYG 100
    QNQWAPDIQY YNGKYWLYYS VSSFGSNTSA IGLASSTSIS SGGWKDEGLV 150
    IRSTSSNNYN AIDPELTFDK DGNPWLAFGS FWSGIKLTKL DKSTMKPTGS 200
    LYSIAARPNN GGALEAPTLT YQNGYYYLMV SFDKCCDGVN STYKIAYGRS 250
    KSITGPYLDK SGKSMLEGGG TILDSGNDQW KGPGGQDIVN GNILVRHAYD 300
    ANDNGIPKLL INDLNWSSGW PSY 323
    Length:323
    Mass (Da):35,446
    Last modified:July 7, 2009 - v3
    Checksum:i0105FB280E83BC69
    GO

    Sequence cautioni

    The sequence CAA99586.1 differs from that shown. Reason: Frameshift at position 308.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti172 – 1721G → D in CAA99586. (PubMed:8969504)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z75208 Genomic DNA. Translation: CAA99586.1 . Frameshift.
    AY669857 Genomic DNA. Translation: AAV87172.1 .
    AL009126 Genomic DNA. Translation: CAB14841.2 .
    PIRi E69580.
    RefSeqi NP_390759.2. NC_000964.3.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UV4 X-ray 1.50 A 31-307 [» ]
    ProteinModelPortali P94522.
    SMRi P94522. Positions 33-323.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224308.BSU28810.

    Protein family/group databases

    CAZyi GH43. Glycoside Hydrolase Family 43.

    Proteomic databases

    PaxDbi P94522.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB14841 ; CAB14841 ; BSU28810 .
    GeneIDi 937430.
    KEGGi bsu:BSU28810.
    PATRICi 18977654. VBIBacSub10457_3015.

    Organism-specific databases

    GenoListi BSU28810. [Micado ]

    Phylogenomic databases

    eggNOGi COG3507.
    HOGENOMi HOG000292006.
    KOi K06113.
    OrthoDBi EOG686NDH.
    PhylomeDBi P94522.

    Enzyme and pathway databases

    UniPathwayi UPA00667 .
    BioCyci BSUB:BSU28810-MONOMER.
    MetaCyc:BSU28810-MONOMER.
    SABIO-RK P94522.

    Miscellaneous databases

    EvolutionaryTracei P94522.

    Family and domain databases

    Gene3Di 2.115.10.20. 1 hit.
    InterProi IPR006710. Glyco_hydro_43.
    IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
    IPR023296. Glyco_hydro_beta-prop.
    [Graphical view ]
    PANTHERi PTHR22925. PTHR22925. 1 hit.
    Pfami PF04616. Glyco_hydro_43. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
    SUPFAMi SSF75005. SSF75005. 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. "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.
      , 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.

    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: October 1, 2014
    This is version 88 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

    External Data

    Dasty 3