ID   ABFA_ASPKW              Reviewed;         628 AA.
AC   Q8NK90; G7XYQ0;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 2.
DT   24-JAN-2024, entry version 74.
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; ORFNames=AKAW_10173;
OS   Aspergillus kawachii (strain NBRC 4308) (White koji mold) (Aspergillus
OS   awamori var. kawachi).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1033177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 26-43 AND 482-494,
RP   SUBCELLULAR LOCATION, INDUCTION, FUNCTION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=NBRC 4308;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 4308;
RX   PubMed=22045919; DOI=10.1128/ec.05224-11;
RA   Futagami T., Mori K., Yamashita A., Wada S., Kajiwara Y., Takashita H.,
RA   Omori T., Takegawa K., Tashiro K., Kuhara S., Goto M.;
RT   "Genome sequence of the white koji mold Aspergillus kawachii IFO 4308, used
RT   for brewing the Japanese distilled spirit shochu.";
RL   Eukaryot. Cell 10:1586-1587(2011).
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.
CC       {ECO:0000269|PubMed:16233515}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 4.0. Stable between pH 3.0 and 7.0.
CC         {ECO:0000269|PubMed:16233515};
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius.
CC         {ECO:0000269|PubMed:16233515};
CC   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16233515}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 51 family. {ECO:0000305}.
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DR   EMBL; AB085903; BAB96815.1; -; Genomic_DNA.
DR   EMBL; DF126487; GAA92059.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8NK90; -.
DR   SMR; Q8NK90; -.
DR   STRING; 1033177.Q8NK90; -.
DR   CAZy; GH51; Glycoside Hydrolase Family 51.
DR   GlyCosmos; Q8NK90; 8 sites, No reported glycans.
DR   VEuPathDB; FungiDB:AKAW_10173; -.
DR   eggNOG; ENOG502QQEX; Eukaryota.
DR   InParanoid; Q8NK90; -.
DR   SABIO-RK; Q8NK90; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000006812; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0046556; F:alpha-L-arabinofuranosidase activity; IDA:UniProtKB.
DR   GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019566; P:arabinose metabolic process; IDA: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   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="Alpha-L-arabinofuranosidase A"
FT                   /id="PRO_0000394598"
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"
FT   CONFLICT        140
FT                   /note="D -> E (in Ref. 1; BAB96815)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   628 AA;  67959 MW;  162C5F34386D5705 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 GQFNYFDNLD RSVPYFIGEY SRWEIDWPNM KGSVSEAVFM IGFERNSDVV
     KMAAYAPLLQ LVNSTQWTPD LIGYTQSPDD IFLSTSYYVQ EMFSRNRGDT IKEVTSDSDF
     GPLYWVASSA GDSYYVKLAN YGSETQDLTV SIPGTSTGKL TVLADNDPDA YNSDTQTLVT
     PSESTVQASN GTFTFSLPAW AVAVLAAN
//