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Protein

Alpha-L-arabinofuranosidase C

Gene

abfC

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Alpha-L-arabinofuranosidase involved in the degradation of arabinoxylan, a major component of plant hemicellulose. Acts only on small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides.1 Publication

Catalytic activityi

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

Pathway: 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.

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
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase

Keywords - Biological processi

Carbohydrate metabolism, Polysaccharide degradation

Enzyme and pathway databases

UniPathwayiUPA00667.

Protein family/group databases

CAZyiGH51. Glycoside Hydrolase Family 51.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-L-arabinofuranosidase C (EC:3.2.1.55)
Short name:
ABF C
Short name:
Arabinosidase C
Gene namesi
Name:abfC
ORF Names:AN1277
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome VIII

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 504Alpha-L-arabinofuranosidase CPRO_0000394616
Signal peptidei1 – ?Sequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi152 – 1521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi269 – 2691N-linked (GlcNAc...)Sequence Analysis
Glycosylationi329 – 3291N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi162425.CADANIAP00001344.

Structurei

3D structure databases

ProteinModelPortaliQ5BDV3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 51 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3534.
HOGENOMiHOG000236895.
InParanoidiQ5BDV3.
KOiK01209.
OMAiSGFLEHL.
OrthoDBiEOG71P2KW.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR010720. Alpha-L-AF_C.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF06964. Alpha-L-AF_C. 1 hit.
[Graphical view]
SMARTiSM00813. Alpha-L-AF_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q5BDV3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTFTKLSEQ EAPGISIHPD RRISKINPNI YAGFAEHMGR CIYGGIYDPG
60 70 80 90 100
NPLSDENGFR KDVLEALKEL KVPVIRYPGG NFTATYHWID GVGPRDQRPA
110 120 130 140 150
RPELAWLGTE TNQFGTDEFL KWCEVLGTEP YLCLNMGTGT LDEALAWVDY
160 170 180 190 200
CNGTRDTYYA NLRRKNGREE PYNVKYWALG NEVWGPWQVE QSTKEEYAHK
210 220 230 240 250
AYQWAKALKL LDPSIELILC GKEGPTSWDY YTLKQTMLPV HSPLSTSAVP
260 270 280 290 300
LIDMHSIHLY TAHSSHLPNV TAPLAAERAI EITSSLIDLA RVENGVPPEQ
310 320 330 340 350
RRPTICFDEW NVWDPIRAEG SKGAEESYNL SDALAVGVWL NVFVRKSKDV
360 370 380 390 400
GMACIAQSVN VISPLMTTKD GIVKQTTWWP LYLFSNYMRG WTISAHISVS
410 420 430 440 450
AYEGETHPKW VRGVKDTPWL DVSATLGEDG YVNVVVINIH EEKGIEAKLD
460 470 480 490 500
GPSGEVTVFT VTGDNPAVTN MKGKEEVGLV ETKWDAQGPY VFPKHSLTLL

RWKA
Length:504
Mass (Da):56,554
Last modified:April 26, 2005 - v1
Checksum:i0E79FD944F10970D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490471 mRNA. Translation: ABF50847.1.
AACD01000017 Genomic DNA. Translation: EAA65870.1.
BN001308 Genomic DNA. Translation: CBF87808.1.
RefSeqiXP_658881.1. XM_653789.1.

Genome annotation databases

EnsemblFungiiCADANIAT00001344; CADANIAP00001344; CADANIAG00001344.
GeneIDi2877053.
KEGGiani:AN1277.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490471 mRNA. Translation: ABF50847.1.
AACD01000017 Genomic DNA. Translation: EAA65870.1.
BN001308 Genomic DNA. Translation: CBF87808.1.
RefSeqiXP_658881.1. XM_653789.1.

3D structure databases

ProteinModelPortaliQ5BDV3.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi162425.CADANIAP00001344.

Protein family/group databases

CAZyiGH51. Glycoside Hydrolase Family 51.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00001344; CADANIAP00001344; CADANIAG00001344.
GeneIDi2877053.
KEGGiani:AN1277.2.

Phylogenomic databases

eggNOGiCOG3534.
HOGENOMiHOG000236895.
InParanoidiQ5BDV3.
KOiK01209.
OMAiSGFLEHL.
OrthoDBiEOG71P2KW.

Enzyme and pathway databases

UniPathwayiUPA00667.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR010720. Alpha-L-AF_C.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF06964. Alpha-L-AF_C. 1 hit.
[Graphical view]
SMARTiSM00813. Alpha-L-AF_C. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  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.

Entry informationi

Entry nameiABFC_EMENI
AccessioniPrimary (citable) accession number: Q5BDV3
Secondary accession number(s): C8VSG2, Q1HFV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 26, 2005
Last modified: June 24, 2015
This is version 62 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

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 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.