ID   ABNA_ASPNC              Reviewed;         321 AA.
AC   A2QT85;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   25-MAY-2022, entry version 72.
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=An09g01190;
OS   Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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; AM270193; CAK49041.1; -; Genomic_DNA.
DR   RefSeq; XP_001393437.1; XM_001393400.2.
DR   AlphaFoldDB; A2QT85; -.
DR   SMR; A2QT85; -.
DR   CAZy; GH43; Glycoside Hydrolase Family 43.
DR   PaxDb; A2QT85; -.
DR   EnsemblFungi; CAK49041; CAK49041; An09g01190.
DR   GeneID; 4983650; -.
DR   KEGG; ang:ANI_1_118084; -.
DR   VEuPathDB; FungiDB:An09g01190; -.
DR   HOGENOM; CLU_009397_5_0_1; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000006706; Chromosome 1L.
DR   GO; GO:0005576; C:extracellular region; IDA:AspGD.
DR   GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IDA:AspGD.
DR   GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:2000895; P:hemicellulose catabolic process; IDA:AspGD.
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; Reference proteome; Secreted; Signal;
KW   Xylan degradation.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..321
FT                   /note="Probable arabinan endo-1,5-alpha-L-arabinosidase A"
FT                   /id="PRO_5000220397"
FT   ACT_SITE        34
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P94522"
FT   ACT_SITE        200
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P94522"
FT   SITE            149
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        295
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   321 AA;  34483 MW;  8D176BE3D62B15F0 CRC64;
     MYRLLSVASV PLLASLVHGY ADPGACSGVC TTHDPGLIRR ESDGTYFLFS TGNKISYVSA
     SSIEGPWTSV GSMLPDGSSI DLDGNDDLWA PDVSYVDGLY YVYYAVSTFG SQDSAIGLAT
     SETMEYGSWT DHGSTGIASS SAKIYNAIDP NLIYADGTYY INFGSFWDDI YQVPMKSTPT
     AAASSSYNLA YDPSGTHAEE GSYMFQYGDY YYLFYSAGIC CGYDTSMPAS GEEYHIKVCR
     STSPTGDFVD SDGTACTDGG GTMVLESHGE VYGPGGQGVY DDPNLGPVLY YHYMNTTIGY
     ADSDAQFGWN TIDFSSGWPV V