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Protein

Alpha-L-arabinofuranosidase B

Gene

abfB

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: -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.

pH dependencei

Optimum pH is 4.8.1 Publication

Temperature dependencei

Optimum temperature is 65 degrees Celsius.1 Publication

Pathwayi: L-arabinan degradation

This protein is involved in the pathway L-arabinan degradation, which is part of Glycan metabolism.
View all proteins of this organism that are known to be involved in the pathway L-arabinan degradation and in Glycan metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei182 – 183Cis-peptide bondBy similarity2
Binding sitei225SubstrateBy similarity1
Active sitei227NucleophileBy similarity1
Binding sitei228Substrate; via amide nitrogenBy similarity1
Binding sitei303Substrate; via amide nitrogenBy similarity1
Active sitei304Proton donorBy similarity1
Binding sitei427SubstrateBy similarity1
Binding sitei429Substrate; via amide nitrogenBy similarity1
Binding sitei430Substrate; via amide nitrogenBy similarity1
Binding sitei446SubstrateBy similarity1
Binding sitei475SubstrateBy similarity1
Binding sitei477Substrate; via amide nitrogenBy similarity1
Binding sitei480Substrate; via amide nitrogenBy similarity1
Binding sitei500SubstrateBy similarity1

GO - Molecular functioni

  • alpha-L-arabinofuranosidase activity Source: UniProtKB

GO - Biological processi

  • arabinan catabolic process Source: UniProtKB-UniPathway
  • arabinose metabolic process Source: UniProtKB
  • L-arabinose metabolic process Source: InterPro
  • pectin catabolic process Source: UniProtKB
  • xylan catabolic process Source: UniProtKB-KW

Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate 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_EMENI

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:AN1571
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000000560 Componenti: Chromosome VII
  • UP000005890 Componenti: Unassembled WGS sequence

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000039460925 – 510Alpha-L-arabinofuranosidase BAdd BLAST486

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi27 ↔ 37By similarity
Disulfide bondi87 ↔ 92By similarity
Glycosylationi89N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi182 ↔ 183By similarity
Disulfide bondi412 ↔ 450By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRIDEiO74288

Expressioni

Inductioni

Expressed in presence of L-arabinol and repressed in presence of glucose and glycerol. Expression is also pH regulated probably through the action of the pacC transcription factor and is higher at acidic pHs.1 Publication

Structurei

3D structure databases

ProteinModelPortaliO74288
SMRiO74288
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni25 – 342CatalyticBy similarityAdd BLAST318
Regioni343 – 510ABDBy similarityAdd BLAST168

Domaini

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

Sequence similaritiesi

Belongs to the glycosyl hydrolase 54 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000187007
InParanoidiO74288
KOiK20844
OMAiYPTRYFR
OrthoDBiEOG092C3Z3T

Family and domain databases

InterProiView protein in InterPro
IPR015289 A-L-arabinofuranosidase_B_cat
IPR038964 ABFB
IPR007934 AbfB_ABD
IPR036195 AbfB_ABD_sf
IPR013320 ConA-like_dom_sf
PANTHERiPTHR39447 PTHR39447, 1 hit
PfamiView protein in Pfam
PF05270 AbfB, 1 hit
PF09206 ArabFuran-catal, 1 hit
SUPFAMiSSF110221 SSF110221, 1 hit
SSF49899 SSF49899, 1 hit

Sequencei

Sequence statusi: Complete.

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

O74288-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTMSRSSRSS VLALALATGS LVAAGPCDIY SSGGTPCIAA HSTTRALYSS
60 70 80 90 100
YNGPLYQVQR ASDGTTTTIT PLSAGGVADA SAQDAFCENT TCLITIIYDQ
110 120 130 140 150
SGNGNDLTQA PPGGFNGPDV GGYDNLAGAI GAPVTLNGKK AYGVFVSPGT
160 170 180 190 200
GYRNNEAIGT ATGDEPEGMY AVLDGTHYND GCCFDYGNAE TSSLDTGNGH
210 220 230 240 250
MEAIYYGTNT AWGYGAGNGP WIMADLENGL FSGQSSDYNA GDPSISYRFV
260 270 280 290 300
TAILKGGPNL WALRGGNAAS GSLSTYYNGI RPTDASGYNP MSKEGAIILG
310 320 330 340 350
IGGDNSVSAQ GTFYEGAMTD GYPDDATENS VQADIVAAKY ATTSLISGPA
360 370 380 390 400
LTVGDTVSLK VTTSGYDTRY IAHTGSTINT QVVSSSSSST LKQQASWTVR
410 420 430 440 450
TGLASTAAAN GCVSFESVDT PGSYIRHSNF ALLLNANDGT KLFSEDATFC
460 470 480 490 500
PQDSFNDDGT NSIRSWNYPT RYWRHYENVL YVASNGGVNT FDAATAFTDD
510
VSWVVADGFA
Length:510
Mass (Da):52,942
Last modified:November 1, 1998 - v1
Checksum:i54011DA6AD3BFC22
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13759 Genomic DNA Translation: CAA74084.1
AACD01000025 Genomic DNA Translation: EAA64278.1
BN001307 Genomic DNA Translation: CBF85134.1
RefSeqiXP_659175.1, XM_654083.1

Genome annotation databases

EnsemblFungiiCADANIAT00008202; CADANIAP00008202; CADANIAG00008202
EAA64278; EAA64278; AN1571.2
GeneIDi2875522
KEGGiani:AN1571.2

Similar proteinsi

Entry informationi

Entry nameiABFB_EMENI
AccessioniPrimary (citable) accession number: O74288
Secondary accession number(s): C8VN12, Q5BD09
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: November 1, 1998
Last modified: May 23, 2018
This is version 89 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

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