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P94522

- EABN1_BACSU

UniProt

P94522 - EABN1_BACSU

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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

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
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
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU28810. [Micado]

Subcellular locationi

Secreted 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
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)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.
InParanoidiP94522.
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

        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 CAA99586.1 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.
InParanoidi P94522.
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

« 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. "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 29, 2014
This is version 89 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