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Q8NK89

- ABFB_ASPKW

UniProt

Q8NK89 - ABFB_ASPKW

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Protein
Alpha-L-arabinofuranosidase B
Gene
abfB, AKAW_08685
Organism
Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus awamori var. kawachi)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Able to hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only in L-arabinofuranosyl oligosaccharides, but also in polysaccharides containing terminal non-reducing L-arabinofuranoses in side chains, like L-arabinan, arabinogalactan and arabinoxylan.2 Publications

Catalytic activityi

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

Kineticsi

  1. KM=0.76 mM for L-arabinofuranose2 Publications

pH dependencei

Optimum pH is 4.0. Stable between pH 3.0 and 7.0.

Temperature dependencei

Optimum temperature is 55 degrees Celsius.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei176 – 1772Cis-peptide bond
Binding sitei219 – 2191Substrate
Active sitei221 – 2211Nucleophile1 Publication
Binding sitei222 – 2221Substrate; via amide nitrogen
Binding sitei223 – 2231Substrate; via amide nitrogen
Binding sitei296 – 2961Substrate; via amide nitrogen
Active sitei297 – 2971Proton donor1 Publication
Binding sitei416 – 4161Substrate
Binding sitei418 – 4181Substrate; via amide nitrogen
Binding sitei419 – 4191Substrate; via amide nitrogen
Binding sitei435 – 4351Substrate
Binding sitei463 – 4631Substrate
Binding sitei465 – 4651Substrate; via amide nitrogen
Binding sitei468 – 4681Substrate; via amide nitrogen
Binding sitei488 – 4881Substrate

GO - Molecular functioni

  1. alpha-L-arabinofuranosidase activity Source: UniProtKB

GO - Biological processi

  1. L-arabinose metabolic process Source: InterPro
  2. arabinan catabolic process Source: UniProtKB-UniPathway
  3. arabinose metabolic process Source: UniProtKB
  4. xylan catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation, Xylan degradation

Enzyme and pathway databases

SABIO-RKQ8NK89.
UniPathwayiUPA00667.

Protein family/group databases

CAZyiCBM42. Carbohydrate-Binding Module Family 42.
GH54. Glycoside Hydrolase Family 54.
mycoCLAPiABF54B_ASPKA.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-L-arabinofuranosidase B (EC:3.2.1.55)
Short name:
ABF B
Short name:
Arabinosidase B
Gene namesi
Name:abfB
ORF Names:AKAW_08685
OrganismiAspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus awamori var. kawachi)
Taxonomic identifieri1033177 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006812: Unassembled WGS sequence

Subcellular locationi

Secreted By similarity 1 Publication

GO - Cellular componenti

  1. extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Biotechnological usei

Contribute to an increase in cereal utilization and formation of aroma in shochu brewing.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi176 – 1772CC → AA: Decreases the affinity toward the substrate.
Mutagenesisi204 – 2041T → A: Reduces thermostability and catalytic activity. 1 Publication
Mutagenesisi221 – 2211E → A: Impairs catalytic activity. 1 Publication
Mutagenesisi297 – 2971D → A: Impairs catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 Reviewed prediction
Add
BLAST
Chaini18 – 499482Alpha-L-arabinofuranosidase B
PRO_0000394606Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi21 ↔ 311 Publication
Disulfide bondi81 ↔ 861 Publication
Glycosylationi83 – 831N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi176 ↔ 1771 Publication
Glycosylationi202 – 2021N-linked (GlcNAc...)1 Publication
Disulfide bondi401 ↔ 4391 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Inductioni

Expressed in the presence of L-arabitol and L-arabinose, and repressed in the presence of sucrose and glucose.1 Publication

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 267
Beta strandi31 – 399
Beta strandi50 – 545
Turni55 – 573
Beta strandi60 – 634
Beta strandi65 – 673
Helixi74 – 807
Turni81 – 833
Beta strandi86 – 916
Turni94 – 974
Beta strandi101 – 1033
Beta strandi107 – 1093
Helixi114 – 1163
Beta strandi121 – 13010
Beta strandi133 – 1408
Beta strandi146 – 1505
Beta strandi161 – 1677
Beta strandi174 – 1763
Beta strandi179 – 1835
Beta strandi196 – 2016
Beta strandi210 – 2123
Beta strandi215 – 2195
Beta strandi224 – 2329
Beta strandi242 – 25110
Beta strandi254 – 2618
Beta strandi264 – 27411
Beta strandi281 – 2833
Beta strandi289 – 2946
Beta strandi304 – 31411
Helixi318 – 33114
Beta strandi333 – 3353
Beta strandi349 – 3546
Beta strandi362 – 3676
Beta strandi370 – 3756
Helixi382 – 3876
Beta strandi390 – 3945
Beta strandi401 – 4099
Beta strandi412 – 4176
Beta strandi420 – 4256
Helixi430 – 4356
Beta strandi438 – 4425
Beta strandi446 – 45611
Beta strandi460 – 4645
Beta strandi467 – 4715
Helixi478 – 4803
Helixi485 – 4884
Beta strandi491 – 4955

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WD3X-ray1.75A19-499[»]
1WD4X-ray2.07A19-499[»]
2D43X-ray2.80A19-499[»]
2D44X-ray2.30A19-499[»]
ProteinModelPortaliQ8NK89.
SMRiQ8NK89. Positions 19-499.

Miscellaneous databases

EvolutionaryTraceiQ8NK89.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 335318Catalytic
Add
BLAST
Regioni336 – 499164ABD
Add
BLAST

Domaini

Organized into two domains: an N-terminal catalytic domain and a C-terminal arabinose-binding domain (ABD).1 Publication

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

OrthoDBiEOG7DFXNQ.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR015289. A-L-arabinofuranosidase_B_cat.
IPR007934. AbfB.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
[Graphical view]
PfamiPF05270. AbfB. 1 hit.
PF09206. ArabFuran-catal. 1 hit.
[Graphical view]
SUPFAMiSSF110221. SSF110221. 1 hit.
SSF49899. SSF49899. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8NK89-1 [UniParc]FASTAAdd to Basket

« Hide

MFSRRNLLAL GLAATVSAGP CDIYEAGDTP CVAAHSTTRA LYSSFSGALY    50
QLQRGSDDTT TTISPLTAGG IADASAQDTF CANTTCLITI IYDQSGNGNH 100
LTQAPPGGFD GPDTDGYDNL ASAIGAPVTL NGQKAYGVFM SPGTGYRNNE 150
ATGTATGDEA EGMYAVLDGT HYNDACCFDY GNAETSSTDT GAGHMEAIYL 200
GNSTTWGYGA GDGPWIMVDM ENNLFSGADE GYNSGDPSIS YRFVTAAVKG 250
GADKWAIRGA NAASGSLSTY YSGARPDYSG YNPMSKEGAI ILGIGGDNSN 300
GAQGTFYEGV MTSGYPSDDT ENSVQENIVA AKYVVGSLVS GPSFTSGEVV 350
SLRVTTPGYT TRYIAHTDTT VNTQVVDDDS STTLKEEASW TVVTGLANSQ 400
CFSFESVDTP GSYIRHYNFE LLLNANDGTK QFHEDATFCP QAALNGEGTS 450
LRSWSYPTRY FRHYENVLYA ASNGGVQTFD SKTSFNNDVS FEIETAFAS 499
Length:499
Mass (Da):52,598
Last modified:October 1, 2002 - v1
Checksum:i94B340130BB18746
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB085904 Genomic DNA. Translation: BAB96816.1.
DF126474 Genomic DNA. Translation: GAA90571.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB085904 Genomic DNA. Translation: BAB96816.1 .
DF126474 Genomic DNA. Translation: GAA90571.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WD3 X-ray 1.75 A 19-499 [» ]
1WD4 X-ray 2.07 A 19-499 [» ]
2D43 X-ray 2.80 A 19-499 [» ]
2D44 X-ray 2.30 A 19-499 [» ]
ProteinModelPortali Q8NK89.
SMRi Q8NK89. Positions 19-499.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi CBM42. Carbohydrate-Binding Module Family 42.
GH54. Glycoside Hydrolase Family 54.
mycoCLAPi ABF54B_ASPKA.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

OrthoDBi EOG7DFXNQ.

Enzyme and pathway databases

UniPathwayi UPA00667 .
SABIO-RK Q8NK89.

Miscellaneous databases

EvolutionaryTracei Q8NK89.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
InterProi IPR015289. A-L-arabinofuranosidase_B_cat.
IPR007934. AbfB.
IPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
[Graphical view ]
Pfami PF05270. AbfB. 1 hit.
PF09206. ArabFuran-catal. 1 hit.
[Graphical view ]
SUPFAMi SSF110221. SSF110221. 1 hit.
SSF49899. SSF49899. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Role of two alpha-L-arabinofuranosidases in arabinoxylan degradation and characteristics of the encoding genes from shochu koji molds, Aspergillus kawachii and Aspergillus awamori."
    Koseki T., Okuda M., Sudoh S., Kizaki Y., Iwano K., Aramaki I., Matsuzawa H.
    J. Biosci. Bioeng. 96:232-241(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 18-27 AND 421-432, SUBCELLULAR LOCATION, INDUCTION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, BIOTECHNOLOGY.
    Strain: NBRC 4308.
  2. "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used for brewing the Japanese distilled spirit shochu."
    Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H., Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.
    Eukaryot. Cell 10:1586-1587(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NBRC 4308.
  3. "Crystal structure of a family 54 alpha-L-arabinofuranosidase reveals a novel carbohydrate-binding module that can bind arabinose."
    Miyanaga A., Koseki T., Matsuzawa H., Wakagi T., Shoun H., Fushinobu S.
    J. Biol. Chem. 279:44907-44914(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 19-499 IN COMPLEX WITH SUBSTRATE, DOMAIN, ACTIVE SITE, DISULFIDE BONDS, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION AT ASN-202, MUTAGENESIS OF 176-CYS-CYS-177; THR-204; GLU-221 AND ASP-297.
    Strain: NBRC 4308.
  4. "The family 42 carbohydrate-binding module of family 54 alpha-L-arabinofuranosidase specifically binds the arabinofuranose side chain of hemicellulose."
    Miyanaga A., Koseki T., Miwa Y., Mese Y., Nakamura S., Kuno A., Hirabayashi J., Matsuzawa H., Wakagi T., Shoun H., Fushinobu S.
    Biochem. J. 399:503-511(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 19-499 OF THE ALA-221 MUTANT IN COMPLEX WITH SUBSTRATE.
    Strain: NBRC 4308.

Entry informationi

Entry nameiABFB_ASPKW
AccessioniPrimary (citable) accession number: Q8NK89
Secondary accession number(s): G7XUM7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: October 1, 2002
Last modified: May 14, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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