ID   ABNA_ASPFN              Reviewed;         319 AA.
AC   B8NDL1;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Probable arabinan endo-1,5-alpha-L-arabinosidase A;
DE            EC=3.2.1.99;
DE   AltName: Full=Endo-1,5-alpha-L-arabinanase A;
DE            Short=ABN A;
DE   Flags: Precursor;
GN   Name=abnA; ORFNames=AFLA_059500;
OS   Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS   / JCM 12722 / SRRC 167).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=332952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 / SRRC
RC   167;
RX   PubMed=25883274; DOI=10.1128/genomea.00168-15;
RA   Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA   Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT   "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT   aflatoxin contamination of food and feed.";
RL   Genome Announc. 3:E0016815-E0016815(2015).
CC   -!- FUNCTION: Endo-1,5-alpha-L-arabinanase involved in degradation of
CC       pectin. Its preferred substrate is linear 1,5-alpha-L-arabinan (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in
CC         (1->5)-arabinans.; EC=3.2.1.99;
CC   -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR   EMBL; EQ963477; EED51687.1; -; Genomic_DNA.
DR   RefSeq; XP_002378694.1; XM_002378653.1.
DR   AlphaFoldDB; B8NDL1; -.
DR   SMR; B8NDL1; -.
DR   EnsemblFungi; EED51687; EED51687; AFLA_059500.
DR   VEuPathDB; FungiDB:AFLA_059500; -.
DR   eggNOG; ENOG502QTQG; Eukaryota.
DR   HOGENOM; CLU_009397_5_0_1; -.
DR   OMA; KNDPWAP; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000001875; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0045493; P:xylan catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.115.10.20; -; 1.
DR   InterPro; IPR006710; Glyco_hydro_43.
DR   InterPro; IPR016840; Glyco_hydro_43_endo_a_Ara-ase.
DR   InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   PIRSF; PIRSF026534; Endo_alpha-L-arabinosidase; 1.
DR   SUPFAM; SSF75005; SSF75005; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal; Xylan degradation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..319
FT                   /note="Probable arabinan endo-1,5-alpha-L-arabinosidase A"
FT                   /id="PRO_0000394619"
FT   ACT_SITE        34
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P94522"
FT   ACT_SITE        198
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P94522"
FT   SITE            147
FT                   /note="Important for catalytic activity, responsible for
FT                   pKa modulation of the active site Glu and correct
FT                   orientation of both the proton donor and substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P94522"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   319 AA;  34094 MW;  5861C4ECF5978DF4 CRC64;
     MYLQSSLALV LLRAAVVHGY ANPGACSGAC NIHDPSLIQN GDGTYYRFST GNNISFASAS
     SIEGPWTALG SVLPGGSSID NSGRYDPWAP DVQKVGDLYY LYYAVSSFGT QESAIGLATS
     ETMEEGTWTD KGSIVTSTTG DQYNAIDANL LVDGSANYLT FGSFWQDIFQ VTLNGDATSS
     TSTPVNVAFD PATTHPVEGA YLYKYGDYYY LFYSWGTCCG YDTSRPAEGE EYKIKVCRSS
     TPTGNFVDAS GVACTDGGGT VVLESHDNVY GPGGQGVYTD PNLGPVLYYH YVDTTIGYAD
     SQKLFGWNAI DFSSGWPSV