ID   ABFA_ASPOR              Reviewed;         629 AA.
AC   Q2U790;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 2.
DT   22-FEB-2023, entry version 75.
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=AO090124000023;
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 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAE62575.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP007165; BAE62575.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001823708.2; XM_001823656.2.
DR   AlphaFoldDB; Q2U790; -.
DR   SMR; Q2U790; -.
DR   STRING; 510516.Q2U790; -.
DR   CAZy; GH51; Glycoside Hydrolase Family 51.
DR   GlyCosmos; Q2U790; 9 sites, No reported glycans.
DR   OrthoDB; 1097767at2759; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000006564; Chromosome 5.
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   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; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
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   SMART; SM00813; Alpha-L-AF_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..629
FT                   /note="Probable alpha-L-arabinofuranosidase A"
FT                   /id="PRO_0000394599"
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        140
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        168
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        171
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        494
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        534
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   629 AA;  68126 MW;  9496AA78282C6549 CRC64;
     MVALSTLSGL SALPFLFSLV QNVYGVSLEV STEKGNSSSP ILYGFMFEDI NHSGDGGIYG
     QLLRNNGLQG SKPGLTAWAA VGDATIAVDA QNPLTEAIPH SLKLDVKQGA SGAVGFTNEG
     YWGVPVDGSE FLNTFWIKGN FSGDITVRLV GNNTGTEYGS TKISQSSNSS NFTKVLAKIP
     TKKAPDGAVL YELTVDGASV GGSSLNFGLF ELFPQTYKSR SNGLKPQVAQ PLADMKGSFL
     RFPGGNNLEG ASEARRWKWN ETIGPVENRP GRQGDWSYYN TDGLGLDEYF YWCEDMGLTP
     VLGVWAGFAL ESGGNTPITG DALKPYIDDV LNELEYVLGD ASTKYGSLRA SYGRKEPWKL
     TMVEIGNEDM LGGGCESYVE RFTAFSDAIH AAYPDLTIIA STDQSSCLPS KLPEGAWVDY
     HNYNTADNLV KQFSQFDNKD RSVPYFIGEY SCQQDNAWPF MQGSVAEAVY MIGIERNSDV
     VKMAAYAPLL QLVNSTQWTP NLIAFTQNPS TVIETTSYYV QQMFSVNRGD TIHNVTSDSA
     FGPVYWVASS ADDKYYVKLA NYGADTQEIT VTISGKTGGK LTVLADSDPK AFNSDTQTLV
     TPSESDMKAT NGKFTFTLPA WSVGVLAAH
//