ID   ABFA_ASPTN              Reviewed;         628 AA.
AC   Q0CTV2;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   04-NOV-2026, entry version 77.
DE   RecName: Full=Probable alpha-L-arabinofuranosidase A;
DE            Short=ABF A;
DE            Short=Arabinosidase A;
DE            EC=3.2.1.55;
DE   Flags: Precursor;
GN   Name=abfA; ORFNames=ATEG_02882;
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 degradation of
CC       arabinoxylan, a major component of plant hemicellulose. Acts only on
CC       small linear 1,5-alpha-linked L-arabinofuranosyl oligosaccharides (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   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family. {ECO:0000305}.
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DR   EMBL; CH476597; EAU36156.1; -; Genomic_DNA.
DR   RefSeq; XP_001212060.1; XM_001212060.1.
DR   SMR; Q0CTV2; -.
DR   STRING; 341663.Q0CTV2; -.
DR   GlyCosmos; Q0CTV2; 9 sites, No reported glycans.
DR   EnsemblFungi; EAU36156; EAU36156; ATEG_02882.
DR   GeneID; 4317643; -.
DR   VEuPathDB; FungiDB:ATEG_02882; -.
DR   eggNOG; ENOG502QQEX; Eukaryota.
DR   HOGENOM; CLU_010060_1_1_1; -.
DR   OMA; AAHRWNM; -.
DR   OrthoDB; 406864at2759; -.
DR   UniPathway; UPA00667; -.
DR   FunFam; 2.60.40.1180:FF:000036; Probable alpha-L-arabinofuranosidase A; 1.
DR   FunFam; 3.20.20.80:FF:000092; Probable alpha-L-arabinofuranosidase A; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR010720; Alpha-L-AF_C.
DR   InterPro; IPR055235; ASD1_cat.
DR   InterPro; IPR017853; GH_hydrolase_sf.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR051563; Glycosyl_Hydrolase_51.
DR   PANTHER; PTHR31776; ALPHA-L-ARABINOFURANOSIDASE 1; 1.
DR   PANTHER; PTHR31776:SF0; ALPHA-L-ARABINOFURANOSIDASE 1; 1.
DR   Pfam; PF06964; Alpha-L-AF_C; 1.
DR   Pfam; PF22848; ASD1_dom; 1.
DR   SMART; SM00813; Alpha-L-AF_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; ISS:UniProtKB.
DR   GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019566; P:arabinose metabolic process; ISS:UniProtKB.
DR   GO; GO:0046373; P:L-arabinose metabolic process; IEA:InterPro.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   AlphaFoldDB; Q0CTV2; -.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT   CHAIN           26..628
FT                   /note="Probable alpha-L-arabinofuranosidase A"
FT                   /id="PRO_0000394600"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        51
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        260
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        359
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        404
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        493
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   628 AA;  68046 MW;  574064EADFD9BB18 CRC64;
     MVAFSTISGL GALSLLFSII ESVDGVSLKV STDGGNSSSP LLYGFMFEDI NHSGDGGIYG
     QMIQNNGLQG SSPNLTAWAS VGDGTISVDT TNPLTAAIPN SLKLDIKPDA TGAVGFTNEG
     YWGIPVDGTE FQNSFWMKGD FSGEITVRLV GNETGTEYGS TTFNQSSSSD DYTKVSVKFP
     TTKAPDGNVL YELTVDGESA QGSSLSFTLF ELFAQTYKSR SNGLKPQLAD ALESVKGSFL
     RFPGGNNLEG NDVETRWKWN ETIGPLENRP GHQGTWGYFN TDGLGLDEYL YWCEDMNLTP
     VLGVWAGFAL ESGGNTPITG DALTPYIEDV LNELEYVLGD PSTTYGKLRA SYGREEPWNV
     TLVEIGNEDN LGGGCESYAE RFTAFYNAIH DAYPDLTLIA STDNASCLPS PLPEGAWVDY
     HNYNTPDELV KQFGMFDNVD RSVPYFIGEY SRWEIPWPNM QGSVAEAVFM IGLERNSDVV
     KMAAYAPLLQ LVNSTQWTPD LISFTQNPNM VIDSTSYYVQ QMFSVNRGDT IKEVTSDSAF
     GPVYWVASSS GSSYYVKLAN YGADTQEVSV SIPGMSSGKL TVLADSDPEA YNSDTQTLVT
     PSESNVQASN GQFSFTLPAW SVAVLTAN
//