ID   ABFA_ASPNG              Reviewed;         628 AA.
AC   P42254;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=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 niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-35 AND 63-77.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=8000538; DOI=10.1099/00221287-140-10-2673;
RA   Flipphi M.J.A., Visser J., van der Veen P., de Graaff L.H.;
RT   "Arabinase gene expression in Aspergillus niger: indications for
RT   coordinated regulation.";
RL   Microbiology 140:2673-2682(1994).
CC   -!- FUNCTION: Acts only on small linear 1,5-alpha-linked L-arabinofuranosyl
CC       oligosaccharides.
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family. {ECO:0000305}.
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DR   EMBL; L29005; AAC41644.1; -; Genomic_DNA.
DR   AlphaFoldDB; P42254; -.
DR   SMR; P42254; -.
DR   STRING; 5061.CADANGAP00000030; -.
DR   CAZy; GH51; Glycoside Hydrolase Family 51.
DR   CLAE; ABF51A_ASPNG; -.
DR   VEuPathDB; FungiDB:An01g00330; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1116622; -.
DR   VEuPathDB; FungiDB:ATCC64974_23190; -.
DR   VEuPathDB; FungiDB:M747DRAFT_331887; -.
DR   eggNOG; ENOG502QQEX; Eukaryota.
DR   BioCyc; MetaCyc:MON-16901; -.
DR   BRENDA; 3.2.1.55; 518.
DR   UniPathway; UPA00667; -.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
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   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000269|PubMed:8000538"
FT   CHAIN           26..628
FT                   /note="Alpha-L-arabinofuranosidase A"
FT                   /id="PRO_0000012216"
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   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        440
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        493
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        610
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   628 AA;  67833 MW;  4F3E476FF93468AD CRC64;
     MVAFSALSGV SAVSLLLSLV QNAHGISLKV STQGGNSSSP ILYGFMFEDI NHSGDGGIYG
     QMLQNPGLQG TAPNLTAWAA VGDATIAIDG DSPLTSAIPS TIKLNIADDA TGAVGLTNEG
     YWGIPVDGSE FHSSFWIKGD YSGDITVRLV GNYTGTEYGS TTITHTSTAD NFTQASVKFP
     TTKAPDGNVL YELTVDGSVA AGSSLNFGYL TLFGETYKSR ENGLKPQLAN VLDDMKGSFL
     RFPGGNNLEG NSAENRWKWN ETIGDLCDRP GREGTWTYYN TDGLGLHEYF YWCEDLGLVP
     VLGVWDGFAL ESGGNTPLTG DALTPYIDDV LNELEYILGD TSTTYGAWRA ANGQEEPWNL
     TMVEIGNEDM LGGGCESYAE RFTAFYDAIH AAYPDLILIA STSEADCLPE SMPEGSWVDY
     HDYSTPDGLV GQFNYFDNLN RSVPYFIGEY SRWEIDWPNM KGSVAEAVFM IGFERNSDVV
     KMAAYAPLLQ LINSTQWTPD LIGYTQSPGD IFLSTSYYVQ EMFSRNRGDT IKEVTSDSDF
     GPLYWVASSA GDSYYVKLAN YGSETQDLTV SIPGTSTGKL TVLADSDPDA YNSDTQTLVT
     PSESTVQASN GTFTFSLPAW AVAVLAAN