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Q8NK89

- ABFB_ASPKW

UniProt

Q8NK89 - ABFB_ASPKW

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Protein

Alpha-L-arabinofuranosidase B

Gene

abfB

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 7.0.2 Publications

Temperature dependencei

Optimum temperature is 55 degrees Celsius.2 Publications

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei176 – 1772Cis-peptide bond
Binding sitei219 – 2191Substrate2 Publications
Active sitei221 – 2211Nucleophile1 Publication
Binding sitei222 – 2221Substrate; via amide nitrogen2 Publications
Binding sitei223 – 2231Substrate; via amide nitrogen2 Publications
Binding sitei296 – 2961Substrate; via amide nitrogen2 Publications
Active sitei297 – 2971Proton donor1 Publication
Binding sitei416 – 4161Substrate2 Publications
Binding sitei418 – 4181Substrate; via amide nitrogen2 Publications
Binding sitei419 – 4191Substrate; via amide nitrogen2 Publications
Binding sitei435 – 4351Substrate2 Publications
Binding sitei463 – 4631Substrate2 Publications
Binding sitei465 – 4651Substrate; via amide nitrogen2 Publications
Binding sitei468 – 4681Substrate; via amide nitrogen2 Publications
Binding sitei488 – 4881Substrate2 Publications

GO - Molecular functioni

  1. alpha-L-arabinofuranosidase activity Source: UniProtKB

GO - Biological processi

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

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. 1 Publication
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 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 499482Alpha-L-arabinofuranosidase BPRO_0000394606Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi21 ↔ 311 Publication
Disulfide bondi81 ↔ 861 Publication
Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
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

1
499
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 267Combined sources
Beta strandi31 – 399Combined sources
Beta strandi50 – 545Combined sources
Turni55 – 573Combined sources
Beta strandi60 – 634Combined sources
Beta strandi65 – 673Combined sources
Helixi74 – 807Combined sources
Turni81 – 833Combined sources
Beta strandi86 – 916Combined sources
Turni94 – 974Combined sources
Beta strandi101 – 1033Combined sources
Beta strandi107 – 1093Combined sources
Helixi114 – 1163Combined sources
Beta strandi121 – 13010Combined sources
Beta strandi133 – 1408Combined sources
Beta strandi146 – 1505Combined sources
Beta strandi161 – 1677Combined sources
Beta strandi174 – 1763Combined sources
Beta strandi179 – 1835Combined sources
Beta strandi196 – 2016Combined sources
Beta strandi210 – 2123Combined sources
Beta strandi215 – 2195Combined sources
Beta strandi224 – 2329Combined sources
Beta strandi242 – 25110Combined sources
Beta strandi254 – 2618Combined sources
Beta strandi264 – 27411Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi289 – 2946Combined sources
Beta strandi304 – 31411Combined sources
Helixi318 – 33114Combined sources
Beta strandi333 – 3353Combined sources
Beta strandi349 – 3546Combined sources
Beta strandi362 – 3676Combined sources
Beta strandi370 – 3756Combined sources
Helixi382 – 3876Combined sources
Beta strandi390 – 3945Combined sources
Beta strandi401 – 4099Combined sources
Beta strandi412 – 4176Combined sources
Beta strandi420 – 4256Combined sources
Helixi430 – 4356Combined sources
Beta strandi438 – 4425Combined sources
Beta strandi446 – 45611Combined sources
Beta strandi460 – 4645Combined sources
Beta strandi467 – 4715Combined sources
Helixi478 – 4803Combined sources
Helixi485 – 4884Combined sources
Beta strandi491 – 4955Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8NK89.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni18 – 335318CatalyticAdd
BLAST
Regioni336 – 499164ABDAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the glycosyl hydrolase 54 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

InParanoidiQ8NK89.
OrthoDBiEOG7DFXNQ.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR015289. A-L-arabinofuranosidase_B_cat.
IPR007934. AbfB.
IPR013320. ConA-like_dom.
[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

        10         20         30         40         50
MFSRRNLLAL GLAATVSAGP CDIYEAGDTP CVAAHSTTRA LYSSFSGALY
60 70 80 90 100
QLQRGSDDTT TTISPLTAGG IADASAQDTF CANTTCLITI IYDQSGNGNH
110 120 130 140 150
LTQAPPGGFD GPDTDGYDNL ASAIGAPVTL NGQKAYGVFM SPGTGYRNNE
160 170 180 190 200
ATGTATGDEA EGMYAVLDGT HYNDACCFDY GNAETSSTDT GAGHMEAIYL
210 220 230 240 250
GNSTTWGYGA GDGPWIMVDM ENNLFSGADE GYNSGDPSIS YRFVTAAVKG
260 270 280 290 300
GADKWAIRGA NAASGSLSTY YSGARPDYSG YNPMSKEGAI ILGIGGDNSN
310 320 330 340 350
GAQGTFYEGV MTSGYPSDDT ENSVQENIVA AKYVVGSLVS GPSFTSGEVV
360 370 380 390 400
SLRVTTPGYT TRYIAHTDTT VNTQVVDDDS STTLKEEASW TVVTGLANSQ
410 420 430 440 450
CFSFESVDTP GSYIRHYNFE LLLNANDGTK QFHEDATFCP QAALNGEGTS
460 470 480 490
LRSWSYPTRY FRHYENVLYA ASNGGVQTFD SKTSFNNDVS FEIETAFAS
Length:499
Mass (Da):52,598
Last modified:October 1, 2002 - v1
Checksum:i94B340130BB18746
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB085904 Genomic DNA. Translation: BAB96816.1.
DF126474 Genomic DNA. Translation: GAA90571.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB085904 Genomic DNA. Translation: BAB96816.1 .
DF126474 Genomic DNA. Translation: GAA90571.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

InParanoidi Q8NK89.
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.
IPR013320. ConA-like_dom.
[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: November 26, 2014
This is version 57 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, Reference proteome

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