ID   AXHA_ASPTU              Reviewed;         332 AA.
AC   P79021;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   22-FEB-2023, entry version 73.
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;
OS   Aspergillus tubingensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-34 AND 233-245,
RP   AND SUBCELLULAR LOCATION.
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 (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:0000269|PubMed:9000377}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 62 family. {ECO:0000305}.
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DR   EMBL; Z78010; CAB01408.1; -; Genomic_DNA.
DR   AlphaFoldDB; P79021; -.
DR   SMR; P79021; -.
DR   CAZy; GH62; Glycoside Hydrolase Family 62.
DR   CLAE; AXH62A_ASPTU; -.
DR   GlyCosmos; P79021; 1 site, No reported glycans.
DR   VEuPathDB; FungiDB:ASPTUDRAFT_40721; -.
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   InterPro; IPR005193; GH62_arabinosidase.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   PANTHER; PTHR40631; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR   PANTHER; PTHR40631:SF1; ALPHA-L-ARABINOFURANOSIDASE AXHA-2-RELATED; 1.
DR   Pfam; PF03664; Glyco_hydro_62; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; 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_0000008035"
FT   CARBOHYD        313
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   332 AA;  36050 MW;  409FA65D4686C143 CRC64;
     MKFFKAKGSL LSSGIYLIAL TPFVNAKCAL PSSYSWSSTD ALATPKSGWT ALKDFTDVVS
     DGKHIVYAST TDEAGNYGSM TFGAFSEWSN MASASQTATP FNAVAPTLFY FKPKSIWVLA
     YQWGSSTFTY RTSQDPTNVN GWSSEQALFT GKISDSSTNA IDQTVIGDDT NMYLFFAGDN
     GKIYRSSMSI NDFPGSFGSQ YEVILSGARN DLFEAVQVYT VDGGEGDTKY LMIVEAIGST
     GHRYFRSFTA SSLGGEWTAQ AASEDQPFAG KANSGATWTE DISHGDLVRN NPDQTMTVDP
     CNLQLLYQGH DPNSSGDYNL LPWKPGVLTL KQ
//