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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: 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.

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
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_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: Partially assembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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...)Sequence 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.
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.
OMAiNIVAAKY.
OrthoDBiEOG092C3Z3T.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR015289. A-L-arabinofuranosidase_B_cat.
IPR007934. AbfB_ABD.
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.

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliO74288.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM42. Carbohydrate-Binding Module Family 42.
GH54. Glycoside Hydrolase Family 54.
mycoCLAPiABF54B_EMENI.

Proteomic databases

PRIDEiO74288.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

HOGENOMiHOG000187007.
InParanoidiO74288.
OMAiNIVAAKY.
OrthoDBiEOG092C3Z3T.

Enzyme and pathway databases

UniPathwayiUPA00667.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
InterProiIPR015289. A-L-arabinofuranosidase_B_cat.
IPR007934. AbfB_ABD.
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.
ProtoNetiSearch...

Entry informationi

Entry nameiABFB_EMENI
AccessioniPrimary (citable) accession number: O74288
Secondary accession number(s): C8VN12, Q5BD09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: November 1, 1998
Last modified: October 5, 2016
This is version 81 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, 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. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.