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Protein

Arabinan endo-1,5-alpha-L-arabinosidase C

Gene

abnC

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

Endo-1,5-alpha-L-arabinanase involved in degradation of pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan.1 Publication

Catalytic activityi

Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in (1->5)-arabinans.

Pathwayi

GO - Molecular functioni

  • arabinan endo-1,5-alpha-L-arabinosidase activity Source: UniProtKB

GO - Biological processi

  • arabinan catabolic process Source: UniProtKB-UniPathway
  • 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

CAZyiGH43. Glycoside Hydrolase Family 43.
mycoCLAPiABN43C_EMENI.

Names & Taxonomyi

Protein namesi
Recommended name:
Arabinan endo-1,5-alpha-L-arabinosidase C (EC:3.2.1.99)
Alternative name(s):
Endo-1,5-alpha-L-arabinanase C
Short name:
ABN C
Gene namesi
Name:abnC
ORF Names:AN8007
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000000560 Componenti: Chromosome II

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1515Sequence AnalysisAdd
BLAST
Chaini16 – 320305Arabinan endo-1,5-alpha-L-arabinosidase CPRO_0000394638Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi126 – 1261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi190 – 1901N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliQ5AUM3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 43 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3507.
HOGENOMiHOG000292006.
InParanoidiQ5AUM3.
KOiK06113.
OMAiNTIDANW.
OrthoDBiEOG761C4Q.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
InterProiIPR006710. Glyco_hydro_43.
IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PANTHERiPTHR22925. PTHR22925. 1 hit.
PfamiPF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
PIRSFiPIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
SUPFAMiSSF75005. SSF75005. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q5AUM3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLALSLFLL SGSLAQYSNP GACSGDCWGH DPGFYQRVSD GRYYRFSTGG
60 70 80 90 100
GIQIHASDNL EGPWEAVGEA LPGGSVVDHA GSTNLWAPDI HYEASTNLYY
110 120 130 140 150
MYYSVSTLGS RDSVIGVATS PNLQPNWTDH GALFRSQAGG NYNAIDANWA
160 170 180 190 200
SIGGSPILTF GSYWNGIHQL PLAGPLSLAD GATPTQIAYN SSGNHAIEAG
210 220 230 240 250
FVFYRRGWYY LTFSSGRAGS YDTNPPATGE EYRIVVCRSA SGTGDFVDKS
260 270 280 290 300
GRSCLTDNGG TTILASHGNV YGPGGQGVFE DRTRGWVLYY HYANPDIGLS
310 320
TGQYQFGWNV LQWADGWPSV
Length:320
Mass (Da):34,374
Last modified:April 26, 2005 - v1
Checksum:i72DFFD05A3CC6C5C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490514 mRNA. Translation: ABF50890.1.
AACD01000138 Genomic DNA. Translation: EAA58810.1.
BN001302 Genomic DNA. Translation: CBF73694.1.
RefSeqiXP_681276.1. XM_676184.1.

Genome annotation databases

EnsemblFungiiCADANIAT00004027; CADANIAP00004027; CADANIAG00004027.
GeneIDi2869148.
KEGGiani:AN8007.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ490514 mRNA. Translation: ABF50890.1.
AACD01000138 Genomic DNA. Translation: EAA58810.1.
BN001302 Genomic DNA. Translation: CBF73694.1.
RefSeqiXP_681276.1. XM_676184.1.

3D structure databases

ProteinModelPortaliQ5AUM3.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH43. Glycoside Hydrolase Family 43.
mycoCLAPiABN43C_EMENI.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00004027; CADANIAP00004027; CADANIAG00004027.
GeneIDi2869148.
KEGGiani:AN8007.2.

Phylogenomic databases

eggNOGiCOG3507.
HOGENOMiHOG000292006.
InParanoidiQ5AUM3.
KOiK06113.
OMAiNTIDANW.
OrthoDBiEOG761C4Q.

Enzyme and pathway databases

UniPathwayiUPA00667.

Family and domain databases

Gene3Di2.115.10.20. 1 hit.
InterProiIPR006710. Glyco_hydro_43.
IPR016840. Glyco_hydro_43_endo_a_Ara-ase.
IPR023296. Glyco_hydro_beta-prop.
[Graphical view]
PANTHERiPTHR22925. PTHR22925. 1 hit.
PfamiPF04616. Glyco_hydro_43. 1 hit.
[Graphical view]
PIRSFiPIRSF026534. Endo_alpha-L-arabinosidase. 1 hit.
SUPFAMiSSF75005. SSF75005. 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 nameiABNC_EMENI
AccessioniPrimary (citable) accession number: Q5AUM3
Secondary accession number(s): C8V5S3, Q1HFR0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: April 26, 2005
Last modified: January 7, 2015
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, 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.