AXHA_ASPNC
ID AXHA_ASPNC Reviewed; 332 AA.
AC A2QFV9;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Probable alpha-L-arabinofuranosidase axhA;
DE EC=3.2.1.55;
DE AltName: Full=Arabinoxylan arabinofuranohydrolase axhA;
DE Flags: Precursor;
GN Name=axhA; ORFNames=An03g00960;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Alpha-L-arabinofuranosidase involved in the hydrolysis of
CC xylan, a major structural heterogeneous polysaccharide found in plant
CC biomass representing the second most abundant polysaccharide in the
CC biosphere, after cellulose. Releases L-arabinose from arabinoxylan (By
CC similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside
CC residues in alpha-L-arabinosides.; EC=3.2.1.55;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 62 family. {ECO:0000305}.
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DR EMBL; AM270045; CAK38069.1; -; Genomic_DNA.
DR RefSeq; XP_001389998.1; XM_001389961.2.
DR AlphaFoldDB; A2QFV9; -.
DR SMR; A2QFV9; -.
DR CAZy; GH62; Glycoside Hydrolase Family 62.
DR PaxDb; A2QFV9; -.
DR EnsemblFungi; CAK38069; CAK38069; An03g00960.
DR GeneID; 4980084; -.
DR KEGG; ang:ANI_1_108034; -.
DR VEuPathDB; FungiDB:An03g00960; -.
DR HOGENOM; CLU_041805_0_0_1; -.
DR Proteomes; UP000006706; Chromosome 6R.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR CDD; cd08987; GH62; 1.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR005193; GH62_arabinosidase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR PANTHER; PTHR40631; PTHR40631; 1.
DR Pfam; PF03664; Glyco_hydro_62; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW Xylan degradation.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..332
FT /note="Probable alpha-L-arabinofuranosidase axhA"
FT /id="PRO_5000219727"
SQ SEQUENCE 332 AA; 35837 MW; F6EEE44EB8C43FEB CRC64;
MKFLKAKGSL LSSGIYLIAL APFVNAKCAL PSTYSWTSTD ALATPKSGWT ALKDFTDVVS
NGKHIVYAST TDTQGNYGSM GFGAFSDWSD MASASQTATS FSAVAPTLFY FQPKSIWVLA
YQWGSSTFTY RTSQDPTNVN GWSSEQALFT GKISGSSTGA IDQTVIGDDT NMYLFFAGDN
GKIYRSSMSI NDFPGSFGSQ YEEILSGATN DLFEAVQVYT VDGGEGDSKY LMIVEAIGST
GHRYFRSFTA SSLGGEWTAQ AASEDQPFAG KANSGATWTD DISHGDLVRN NPDQTMTVDP
CNLQLLYQGH DPNSNSDYNL LPWKPGVLTL KQ