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O74288

- ABFB_EMENI

UniProt

O74288 - ABFB_EMENI

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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: 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei182 – 1832Cis-peptide bondBy similarity
Binding sitei225 – 2251SubstrateBy similarity
Active sitei227 – 2271NucleophileBy similarity
Binding sitei228 – 2281Substrate; via amide nitrogenBy similarity
Binding sitei303 – 3031Substrate; via amide nitrogenBy similarity
Active sitei304 – 3041Proton donorBy similarity
Binding sitei427 – 4271SubstrateBy similarity
Binding sitei429 – 4291Substrate; via amide nitrogenBy similarity
Binding sitei430 – 4301Substrate; via amide nitrogenBy similarity
Binding sitei446 – 4461SubstrateBy similarity
Binding sitei475 – 4751SubstrateBy similarity
Binding sitei477 – 4771Substrate; via amide nitrogenBy similarity
Binding sitei480 – 4801Substrate; via amide nitrogenBy similarity
Binding sitei500 – 5001SubstrateBy 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. pectin catabolic process Source: UniProtKB
  5. 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
ProteomesiUP000000560: Chromosome VII

Subcellular locationi

Secreted 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 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 510486Alpha-L-arabinofuranosidase BPRO_0000394609Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi27 ↔ 37By similarity
Disulfide bondi87 ↔ 92By similarity
Glycosylationi89 – 891N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi182 ↔ 183By similarity
Disulfide bondi412 ↔ 450By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

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

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00008202.

Structurei

3D structure databases

ProteinModelPortaliO74288.
SMRiO74288. Positions 25-510.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni25 – 342318CatalyticBy similarityAdd
BLAST
Regioni343 – 510168ABDBy similarityAdd
BLAST

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

eggNOGiNOG83819.
HOGENOMiHOG000187007.
InParanoidiO74288.
OMAiNIVAAKY.
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.

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.
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 .
RefSeqi XP_659175.1. XM_654083.1.

3D structure databases

ProteinModelPortali O74288.
SMRi O74288. Positions 25-510.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 162425.CADANIAP00008202.

Protein family/group databases

CAZyi CBM42. Carbohydrate-Binding Module Family 42.
GH54. Glycoside Hydrolase Family 54.
mycoCLAPi ABF54B_EMENI.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANIAT00008202 ; CADANIAP00008202 ; CADANIAG00008202 .
GeneIDi 2875522.
KEGGi ani:AN1571.2.

Phylogenomic databases

eggNOGi NOG83819.
HOGENOMi HOG000187007.
InParanoidi O74288.
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.
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. "The abfB gene encoding the major alpha-L-arabinofuranosidase of Aspergillus nidulans: nucleotide sequence, regulation and construction of a disrupted strain."
    Gielkens M., Gonzalez-Candelas L., Sanchez-Torres P., van de Vondervoort P., de Graaff L., Visser J., Ramon D.
    Microbiology 145:735-741(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION, SUBCELLULAR LOCATION, FUNCTION.
    Strain: ArgB2, biA1 and MetG1.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  4. "Development and application of a suite of polysaccharide-degrading enzymes for analyzing plant cell walls."
    Bauer S., Vasu P., Persson S., Mort A.J., Somerville C.R.
    Proc. Natl. Acad. Sci. U.S.A. 103:11417-11422(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

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 29, 2014
This is version 72 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

External Data

Dasty 3