ID   AXHA_ASPTN              Reviewed;         326 AA.
AC   Q0C8B3;
DT   20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 57.
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=ATEG_10071;
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156;
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CH476609; EAU29520.1; -; Genomic_DNA.
DR   RefSeq; XP_001209373.1; XM_001209373.1.
DR   AlphaFoldDB; Q0C8B3; -.
DR   SMR; Q0C8B3; -.
DR   STRING; 341663.Q0C8B3; -.
DR   EnsemblFungi; EAU29520; EAU29520; ATEG_10071.
DR   GeneID; 4319554; -.
DR   VEuPathDB; FungiDB:ATEG_10071; -.
DR   eggNOG; ENOG502QUZT; Eukaryota.
DR   HOGENOM; CLU_041805_0_0_1; -.
DR   OMA; FAPKDIW; -.
DR   OrthoDB; 814559at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..326
FT                   /note="Probable alpha-L-arabinofuranosidase axhA"
FT                   /id="PRO_0000393535"
FT   CARBOHYD        307
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   326 AA;  35088 MW;  9B391295A16C4943 CRC64;
     MRPRQSKVTQ VLSGAVLLAS GAAASCSLPS TYSWTSTEAL AEPKSGWTAL KDFTNVVSNG
     QHIVYASTTD SSGNYGSMAF SPFADWSDMA SASQNAMSAS AVAPTIFYFA PKDVWILAYQ
     WGPTAFSYKT SSDPSDANGW SEAQPLFSGS ISDSSTGVID QTVIGDDTNM YLFFAGDNGR
     IYRASMSIDN FPGDFGTQSE VVLEDTTNNL FEAVQVYKVD GQDQYLMIVE AIGSAGRYFR
     SFTASSLDGE WTVQAGTEDQ PFAGKANSGA SWTNDISHGD LVRNNPDQTF TVDPCNLQLL
     YQGKDPNSSG DYNQLAWRPG VLTLKV