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Q2UIM2

- ABFB_ASPOR

UniProt

Q2UIM2 - ABFB_ASPOR

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Protein

Alpha-L-arabinofuranosidase B

Gene
abfB, AO090023000001
Organism
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Status
Reviewed - Annotation score: 4 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.1 Publication

Catalytic activityi

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

pH dependencei

Optimum pH is 5.5. Stable between pH 4.0 and 6.5.1 Publication

Temperature dependencei

Optimum temperature is 60 degrees Celsius.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei184 – 1852Cis-peptide bond By similarity
Binding sitei227 – 2271Substrate By similarity
Active sitei229 – 2291Nucleophile By similarity
Binding sitei230 – 2301Substrate; via amide nitrogen By similarity
Binding sitei304 – 3041Substrate; via amide nitrogen By similarity
Active sitei305 – 3051Proton donor By similarity
Binding sitei424 – 4241Substrate By similarity
Binding sitei426 – 4261Substrate; via amide nitrogen By similarity
Binding sitei427 – 4271Substrate; via amide nitrogen By similarity
Binding sitei443 – 4431Substrate By similarity
Binding sitei471 – 4711Substrate By similarity
Binding sitei473 – 4731Substrate; via amide nitrogen By similarity
Binding sitei476 – 4761Substrate; via amide nitrogen By similarity
Binding sitei496 – 4961Substrate By similarity

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

UniPathwayiUPA00667.

Protein family/group databases

CAZyiCBM42. Carbohydrate-Binding Module Family 42.
GH54. Glycoside Hydrolase Family 54.
mycoCLAPiABF54B_ASPOR.

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:AO090023000001
OrganismiAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Taxonomic identifieri510516 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006564: Chromosome 3

Subcellular locationi

Secreted By similarity 1 Publication

GO - Cellular componenti

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

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626 Reviewed predictionAdd
BLAST
Chaini27 – 506480Alpha-L-arabinofuranosidase BPRO_0000394607Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi29 ↔ 39 By similarity
Disulfide bondi89 ↔ 94 By similarity
Glycosylationi91 – 911N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi184 ↔ 185 By similarity
Disulfide bondi409 ↔ 447 By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Expressioni

Inductioni

Repressed by glucose.1 Publication

Interactioni

Protein-protein interaction databases

STRINGi5062.CADAORAP00007019.

Structurei

3D structure databases

ProteinModelPortaliQ2UIM2.
SMRiQ2UIM2. Positions 27-506.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni27 – 343317Catalytic By similarityAdd
BLAST
Regioni344 – 506163ABD By similarityAdd
BLAST

Domaini

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

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG83819.
HOGENOMiHOG000187007.
OMAiNIVAAKY.
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.

Q2UIM2-1 [UniParc]FASTAAdd to Basket

« Hide

MSSGLSLERA CAVALGIVAS ASLVAAGPCD IYSSGGTPCV AAHSTTRALY    50
SAYTGALYQV KRGSDGSTTD IAPLSAGGVA DAAIQDSFCA NTTCLITIIY 100
DQSGRGNHLT QAPPGGFNGP ESNGYDNLAS AVGAPVTLNG KKAYGVFMSP 150
GTGYRNNAAS GTATGDKAEG MYAVLDGTHY NSACCFDYGN AEVSNTDTGN 200
GHMEAIYYGD NTVWGSGAGS GPWIMADLEN GLFSGLSSTN NAGDPSISYR 250
FVTAVVKGEA NQWSIRGANA ASGSLSTYYS GARPSASGYN PMSKEGAIIL 300
GIGGDNSNGA QGTFYEGVMT SGYPSDATEN SVQADIVAAK YAIASLTSGP 350
ALTVGSSISL QVTTAGYTTR YLAHDGSTVN TQVVSSSSTT ALRQQASWTV 400
RTGLANSACL SFESVDTPGS YIRHYNFALL LNANDGTKQF YEDATFCPQA 450
GLNGQGNSIR SWSYPTRYFR HYENVLYVAS NGGVQTFDAT TSFNDDVSWV 500
VSTGFA 506
Length:506
Mass (Da):52,195
Last modified:January 24, 2006 - v1
Checksum:iA0D6B300C19C9420
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461T → A in BAB71804. 1 Publication
Sequence conflicti84 – 841I → T in BAB71803. 1 Publication
Sequence conflicti167 – 1671K → E in BAB71803. 1 Publication
Sequence conflicti387 – 3871S → T in BAB71803. 1 Publication
Sequence conflicti390 – 3901T → K in BAB71803. 1 Publication
Sequence conflicti393 – 3931R → K in BAB71803. 1 Publication
Sequence conflicti410 – 4101L → F in BAB71803. 1 Publication
Sequence conflicti429 – 4291L → H in BAB71803. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB073860 Genomic DNA. Translation: BAB71803.1.
AB073861 Genomic DNA. Translation: BAB71804.1.
AP007157 Genomic DNA. Translation: BAE58593.1.
RefSeqiXP_001820595.1. XM_001820543.1.

Genome annotation databases

EnsemblFungiiCADAORAT00007157; CADAORAP00007019; CADAORAG00007157.
GeneIDi5993498.
KEGGiaor:AOR_1_144.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB073860 Genomic DNA. Translation: BAB71803.1 .
AB073861 Genomic DNA. Translation: BAB71804.1 .
AP007157 Genomic DNA. Translation: BAE58593.1 .
RefSeqi XP_001820595.1. XM_001820543.1.

3D structure databases

ProteinModelPortali Q2UIM2.
SMRi Q2UIM2. Positions 27-506.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5062.CADAORAP00007019.

Protein family/group databases

CAZyi CBM42. Carbohydrate-Binding Module Family 42.
GH54. Glycoside Hydrolase Family 54.
mycoCLAPi ABF54B_ASPOR.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADAORAT00007157 ; CADAORAP00007019 ; CADAORAG00007157 .
GeneIDi 5993498.
KEGGi aor:AOR_1_144.

Phylogenomic databases

eggNOGi NOG83819.
HOGENOMi HOG000187007.
OMAi NIVAAKY.
OrthoDBi EOG7DFXNQ.

Enzyme and pathway databases

UniPathwayi UPA00667 .

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. "Synergistic degradation of arabinoxylan with alpha-L-arabinofuranosidase, xylanase and beta-xylosidase from soy sauce koji mold, Aspergillus oryzae, in high salt condition."
    Hashimoto T., Nakata Y.
    J. Biosci. Bioeng. 95:164-169(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, INDUCTION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: ATCC 42149 / RIB 40 and HL15.
  2. "Genome sequencing and analysis of Aspergillus oryzae."
    Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K., Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H., Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.
    , Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D., Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A., Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y., Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H., Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T., Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O., Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y., Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N., Kikuchi H.
    Nature 438:1157-1161(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 42149 / RIB 40.

Entry informationi

Entry nameiABFB_ASPOR
AccessioniPrimary (citable) accession number: Q2UIM2
Secondary accession number(s): Q96VA0, Q96VA1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: January 24, 2006
Last modified: May 14, 2014
This is version 55 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

Complete proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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