ID   AXHA_ASPOR              Reviewed;         328 AA.
AC   Q2U7D2;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   25-MAY-2022, entry version 67.
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=AO090701000885;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007164; BAE62533.1; -; Genomic_DNA.
DR   RefSeq; XP_001823666.1; XM_001823614.1.
DR   AlphaFoldDB; Q2U7D2; -.
DR   SMR; Q2U7D2; -.
DR   STRING; 510516.Q2U7D2; -.
DR   CAZy; GH62; Glycoside Hydrolase Family 62.
DR   EnsemblFungi; BAE62533; BAE62533; AO090701000885.
DR   GeneID; 5995723; -.
DR   KEGG; aor:AO090701000885; -.
DR   VEuPathDB; FungiDB:AO090701000885; -.
DR   HOGENOM; CLU_041805_0_0_1; -.
DR   OMA; FAPKDIW; -.
DR   Proteomes; UP000006564; Chromosome 5.
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; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..328
FT                   /note="Probable alpha-L-arabinofuranosidase axhA"
FT                   /id="PRO_0000393534"
FT   CARBOHYD        309
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   328 AA;  35364 MW;  45C65D129AAAA8D1 CRC64;
     MKVTKKVLDQ SLCCTALLAL VGGAAAQCAL PSSYSWTSTG ALAEPKAGWA ALKDFTNVVF
     NGQHIVYGSV ADTSGNYGSM NFGPFSDWSE MASASQNAMN QGTVAPTLFY FAPKDVWILA
     YQWGPTSFSY KTSSDPTDAN GWSAAQPLFS GTISDSDTGV IDQTVIGDDT NMYLFFAGDN
     GKIYRASMPI DNFPGDFGTQ SEIILSDTKE NLFEAVQVYT VDGQNKYLMI VEAMGANGRY
     FRSFTADSLD GEWTVQAGTE SQPFAGKANS GATWTNDISH GDLVRNNPDQ TMTVDPCNLQ
     LLYQGRDPNA SGDYNLLPWK PGVLTLQV