ID   ABFB_ASPNG              Reviewed;         499 AA.
AC   P42255;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Alpha-L-arabinofuranosidase B;
DE            Short=ABF B;
DE            Short=Arabinosidase B;
DE            EC=3.2.1.55;
DE   Flags: Precursor;
GN   Name=abfB;
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 19-30; 221-234;
RP   285-304 AND 312-324.
RC   STRAIN=ATCC 9029 / NRRL 3 / CBS 120.49 / DSM 2466 / N400 / FGSC 732;
RX   PubMed=8299175; DOI=10.1007/bf00351717;
RA   Flipphi M.J.A., van Heuvel M., van der Veen P., Visser J., de Graaff L.H.;
RT   "Cloning and characterization of the abfB gene coding for the major alpha-
RT   L-arabinofuranosidase (ABF B) of Aspergillus niger.";
RL   Curr. Genet. 24:525-532(1993).
CC   -!- FUNCTION: Able to hydrolyze 1,5-, 1,3- and 1,2-alpha-linkages not only
CC       in L-arabinofuranosyl oligosaccharides, but also in polysac-charides
CC       containing terminal non-reducing L-arabinofuranoses in side chains,
CC       like L-arabinan, arabinogalactan and arabinoxylan.
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   -!- INDUCTION: By growth on polymeric substrates and L-arabitol.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 54 family. {ECO:0000305}.
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DR   EMBL; L23502; AAB53944.1; -; Genomic_DNA.
DR   PIR; S39113; S39113.
DR   AlphaFoldDB; P42255; -.
DR   SMR; P42255; -.
DR   STRING; 5061.CADANGAP00011686; -.
DR   CAZy; CBM42; Carbohydrate-Binding Module Family 42.
DR   CAZy; GH54; Glycoside Hydrolase Family 54.
DR   CLAE; ABF54B_ASPNG; -.
DR   VEuPathDB; FungiDB:An15g02300; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1183516; -.
DR   VEuPathDB; FungiDB:ATCC64974_30860; -.
DR   VEuPathDB; FungiDB:M747DRAFT_364642; -.
DR   eggNOG; ENOG502QS3Q; Eukaryota.
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   InterPro; IPR015289; A-L-arabinofuranosidase_B_cat.
DR   InterPro; IPR038964; ABFB.
DR   InterPro; IPR007934; AbfB_ABD.
DR   InterPro; IPR036195; AbfB_ABD_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   PANTHER; PTHR39447; PTHR39447; 1.
DR   Pfam; PF05270; AbfB; 1.
DR   Pfam; PF09206; ArabFuran-catal; 1.
DR   SUPFAM; SSF110221; SSF110221; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycoprotein; Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000269|PubMed:8299175"
FT   CHAIN           19..499
FT                   /note="Alpha-L-arabinofuranosidase B"
FT                   /id="PRO_0000012223"
FT   CARBOHYD        83
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        202
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   499 AA;  52523 MW;  F1F6C3B47AA419C9 CRC64;
     MFSRRNLVAL GLAATVSAGP CDIYEAGDTP CVAAHSTTRA LYSSFSGALY QLQRGSDDTT
     TTISPLTAGG VADASAQDTF CANTTCLITI IYDQSGNGNH LTQAPPGGFD GPDVDGYDNL
     ASAIGAPVTL NGQKAYGVFM SPGTGYRNNE ATGTATGDEP EGMYAVLDGT HYNDACCFDY
     GNAETSSTDT GAGHMEAIYL GNSTTWGYGA GDGPWIMVDM ENNLFSGADE GYNSGDPSIS
     YSFVTAAVKG GADKWAIRGG NAASGSLSTY YSGARPDYSG YNPMSKEGAI ILGIGGDNSN
     GAQGTFYEGV MTSGYPSDDV ENSVQENIVA AKYVSGSLVS GPSFTSGEVV SLRVTTPGYT
     TRYIAHTDTT VNTQVVDDDS STTLKEEASW TVVTGLANSQ CFSFESVDTP GSYIRHYNFE
     LLLNANDGTK QFHEDATFCP QAPLNGEGTS LRSWSYPTRY FRHYENVLYA ASNGGVQTFD
     SKTSFNNDVS FEIETAFAS