ID   AXHA_ASPNG              Reviewed;         332 AA.
AC   P79019;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Alpha-L-arabinofuranosidase axhA;
DE            EC=3.2.1.55;
DE   AltName: Full=Arabinoxylan arabinofuranohydrolase axhA;
DE   Flags: Precursor;
GN   Name=axhA;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=9000377; DOI=10.1007/s002940050172;
RA   Gielkens M.M.C., Visser J., de Graaff L.H.;
RT   "Arabinoxylan degradation by fungi: characterization of the arabinoxylan-
RT   arabinofuranohydrolase encoding genes from Aspergillus niger and
RT   Aspergillus tubingensis.";
RL   Curr. Genet. 31:22-29(1997).
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.
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:0000269|PubMed:9000377}.
CC   -!- INDUCTION: Mainly expressed when grown on xylan and much less on L-
CC       arabitol, L-arabinose and D-xylose. Expression is under the control of
CC       the carbon catabolite repressor creA. {ECO:0000269|PubMed:9000377}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 62 family. {ECO:0000305}.
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DR   EMBL; Z78011; CAB01409.1; -; Genomic_DNA.
DR   AlphaFoldDB; P79019; -.
DR   SMR; P79019; -.
DR   STRING; 5061.CADANGAP00003042; -.
DR   CAZy; GH62; Glycoside Hydrolase Family 62.
DR   CLAE; AXH62A_ASPNG; -.
DR   VEuPathDB; FungiDB:An03g00960; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1159267; -.
DR   VEuPathDB; FungiDB:ATCC64974_83160; -.
DR   VEuPathDB; FungiDB:M747DRAFT_296414; -.
DR   eggNOG; ENOG502QUZT; Eukaryota.
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   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..332
FT                   /note="Alpha-L-arabinofuranosidase axhA"
FT                   /id="PRO_0000008034"
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