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A2QQ94

- ABFC_ASPNC

UniProt

A2QQ94 - ABFC_ASPNC

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Protein

Probable alpha-L-arabinofuranosidase C

Gene

abfC

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 2 out of 5- Protein inferred from homologyi

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 (By similarity).By similarity

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  1. alpha-L-arabinofuranosidase activity Source: UniProtKB-EC

GO - Biological processi

  1. arabinan catabolic process Source: UniProtKB-UniPathway
  2. L-arabinose metabolic process Source: InterPro
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:
Probable alpha-L-arabinofuranosidase C (EC:3.2.1.55)
Short name:
ABF C
Short name:
Arabinosidase C
Gene namesi
Name:abfC
ORF Names:An08g01710
OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
Taxonomic identifieri425011 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000006706: Chromosome 8R

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 505Probable alpha-L-arabinofuranosidase CPRO_0000394614
Signal peptidei1 – ?Sequence Analysis

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi152 – 1521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi181 – 1811N-linked (GlcNAc...)Sequence Analysis
Glycosylationi269 – 2691N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Interactioni

Protein-protein interaction databases

STRINGi5061.CADANGAP00006368.

Structurei

3D structure databases

ProteinModelPortaliA2QQ94.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 51 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiCOG3534.
HOGENOMiHOG000236895.
KOiK01209.
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.

A2QQ94-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTTFTKLSDQ DAPSISIHPA RRLSKINPNI YAGFTEHMGR CIYGGIYDPG
60 70 80 90 100
NSLSDENGFR KDVLEALKEL NIPVVRYPGG NFMATYHWID GVGPKEKRPA
110 120 130 140 150
RPELAWLGTE TNQFGTDEFL KWCEVLGTEP YFCLNFGTGT LDEALAWVEY
160 170 180 190 200
CNGTKDTYYA NLRRKNGREE PYNVKYWALG NETWGPWQVE QMTKEAYAHK
210 220 230 240 250
AYQWAKALKL LDPSLILILC GQDGTASWDY YTLKQCLLPA HSPLSTSTVP
260 270 280 290 300
LIDMHSIHLY TSSPSHLPNV TAPLAAERAI EITSSLIDLA RIENGVPPDQ
310 320 330 340 350
HRPTICFDEW NVWDPIRAEG SKGAEESYTL SDALAVAVFL NVFVRKSKDL
360 370 380 390 400
GMACIAQSVN VISPLMTSKD GITKQTTYWP LYLFSKYMRG WTISVHLSCA
410 420 430 440 450
SYEGETSPKW VRGVKDTPWL DVSATLGEDG YVNVAVVNIH EEKDIRSSID
460 470 480 490 500
GPSGTVSVFT VTGERVQACN MNGKEEVAVT ESTWEAREQF VFPKHSLTLL

RWKLA
Length:505
Mass (Da):56,636
Last modified:March 6, 2007 - v1
Checksum:i3ACDD463A8BB24AE
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270160 Genomic DNA. Translation: CAK39851.1.
RefSeqiXP_001392290.1. XM_001392253.1.

Genome annotation databases

EnsemblFungiiCADANGAT00006491; CADANGAP00006368; CADANGAG00006491.
GeneIDi4982486.
KEGGiang:ANI_1_1698074.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AM270160 Genomic DNA. Translation: CAK39851.1 .
RefSeqi XP_001392290.1. XM_001392253.1.

3D structure databases

ProteinModelPortali A2QQ94.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 5061.CADANGAP00006368.

Protein family/group databases

CAZyi GH51. Glycoside Hydrolase Family 51.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii CADANGAT00006491 ; CADANGAP00006368 ; CADANGAG00006491 .
GeneIDi 4982486.
KEGGi ang:ANI_1_1698074.

Phylogenomic databases

eggNOGi COG3534.
HOGENOMi HOG000236895.
KOi K01209.
OrthoDBi EOG71P2KW.

Enzyme and pathway databases

UniPathwayi UPA00667 .

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR010720. Alpha-L-AF_C.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF06964. Alpha-L-AF_C. 1 hit.
[Graphical view ]
SMARTi SM00813. Alpha-L-AF_C. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
    Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
    , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
    Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CBS 513.88 / FGSC A1513.

Entry informationi

Entry nameiABFC_ASPNC
AccessioniPrimary (citable) accession number: A2QQ94
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: March 6, 2007
Last modified: October 29, 2014
This is version 45 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