ID   ABFA_ASPAW              Reviewed;         628 AA.
AC   Q96X54;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 60.
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;
OS   Aspergillus awamori (Black koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=105351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-43.
RC   STRAIN=ATCC 38854 / NBRC 4033;
RX   PubMed=16233515; DOI=10.1016/s1389-1723(03)80187-1;
RA   Koseki T., Okuda M., Sudoh S., Kizaki Y., Iwano K., Aramaki I.,
RA   Matsuzawa H.;
RT   "Role of two alpha-L-arabinofuranosidases in arabinoxylan degradation and
RT   characteristics of the encoding genes from shochu koji molds, Aspergillus
RT   kawachii and Aspergillus awamori.";
RL   J. Biosci. Bioeng. 96:232-241(2003).
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; AB046702; BAB21568.2; -; Genomic_DNA.
DR   AlphaFoldDB; Q96X54; -.
DR   SMR; Q96X54; -.
DR   CAZy; GH51; Glycoside Hydrolase Family 51.
DR   CLAE; ABF51A_ASPAW; -.
DR   UniPathway; UPA00667; -.
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; 2.60.40.1180; -; 1.
DR   InterPro; IPR010720; Alpha-L-AF_C.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF06964; Alpha-L-AF_C; 1.
DR   SMART; SM00813; Alpha-L-AF_C; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Direct protein sequencing; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:16233515"
FT   CHAIN           26..628
FT                   /note="Probable alpha-L-arabinofuranosidase A"
FT                   /id="PRO_0000394596"
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        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        359
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;  68007 MW;  84E4AF25C4805BE4 CRC64;
     MVAFSALSGV SALSLLLCLV QHAHGVSLKV STQGGNSSSP ILYGFMFEDI NHSGDGGIYG
     QLLQNPGLQG TTPNLTAWAA VGDATIAIDG DSPLTSAIPS TIKLDVADDA TGAVGLTNEG
     YWGIPVDGSE FQSSFWIKGD YSGDITVRLV GNYTGTEYGS ATITHTSTAD NFTQASVKFP
     TTKAPDGNVL YELTVDGSVA AGSSLNFGYL TLFGETYKSR ENGLKPQLAN VLADMKGSFL
     RFPGGNNLEG NSAENRWKWN ETIGDLWDRP GREGTWTYYN TDGLGLHEYF YWCEDLGLVP
     VLGVWDGFAL ESGGNTPITG DALTPYIDDV LNELEYILGD TSTTYGAWRA ANGQEEPWNL
     TMVEIGNEDM LGGGCESYAE RFTAFYDAIH AAYPDLILIA STSEADCLPE SMPEGSWVDY
     HDYSTPDGLV GQFNYFDNLY RSVPYFIGEY SRWEIDWPNM KGSVSEAVFM IGFERNSDVV
     KMAAYAPLLQ LVNSTQWTPD LIGYTQSPDD IFLSTSYYVQ EMFSRNRGDT IKEVTSDSDF
     GPLYWVASSA GDSYYVKLAN YGSETQDLTV SIPGTSTGKL TVLADNDPDA YNSDTQTLVT
     PSESTVQASN GTFTFSLPAW AVAVLAAN