ID   ABNC_ASPNC              Reviewed;         318 AA.
AC   A5AAG2;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=Probable arabinan endo-1,5-alpha-L-arabinosidase C;
DE            EC=3.2.1.99;
DE   AltName: Full=Endo-1,5-alpha-L-arabinanase C;
DE            Short=ABN C;
DE   Flags: Precursor;
GN   Name=abnC; ORFNames=An02g10550;
OS   Aspergillus niger (strain ATCC MYA-4892 / 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=ATCC MYA-4892 / CBS 513.88 / FGSC A1513;
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; AM270026; CAK44404.1; -; Genomic_DNA.
DR   RefSeq; XP_001400184.1; XM_001400147.2.
DR   AlphaFoldDB; A5AAG2; -.
DR   SMR; A5AAG2; -.
DR   CAZy; GH43; Glycoside Hydrolase Family 43.
DR   GlyCosmos; A5AAG2; 4 sites, No reported glycans.
DR   EnsemblFungi; CAK44404; CAK44404; An02g10550.
DR   GeneID; 4979546; -.
DR   KEGG; ang:An02g10550; -.
DR   VEuPathDB; FungiDB:An02g10550; -.
DR   HOGENOM; CLU_009397_5_0_1; -.
DR   OrthoDB; 2655644at2759; -.
DR   UniPathway; UPA00667; -.
DR   Proteomes; UP000006706; Chromosome 4R.
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   CDD; cd18831; GH43_AnAbnA-like; 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   PANTHER; PTHR43301; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE; 1.
DR   PANTHER; PTHR43301:SF7; ARABINAN ENDO-1,5-ALPHA-L-ARABINOSIDASE C; 1.
DR   Pfam; PF04616; Glyco_hydro_43; 1.
DR   PIRSF; PIRSF026534; Endo_alpha-L-arabinosidase; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 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..28
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..318
FT                   /note="Probable arabinan endo-1,5-alpha-L-arabinosidase C"
FT                   /id="PRO_5000242344"
FT   ACT_SITE        30
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P94522"
FT   ACT_SITE        196
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P94522"
FT   SITE            145
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        72
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        80
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        277
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   318 AA;  34047 MW;  E90B7BEBFF22EEE3 CRC64;
     MLSFVLLLCV ALVNAYSDPG ACSGTCWAHD PNVIRRVSDG TYFRFSTGGG VHISSASAIT
     GPWTDLGYAL PNGSIVTVGN ASNLWAPDVH YVDGTYYMYY ASSTLGSRDS TIGVATSTTL
     EADSWTDHGE IGVTSSSSTP YNAIDPNWIT IGSTPYLQFG SYWQGLYQVE MTDSLSASSS
     TPTNLAYNAS GNHAIEASYL YEYGGYYYLT FSSGKAQGYT TSLPAQGDEY RIVVCRSKTG
     TGNFVDKDGV SCLNSGGTTV LASHDYVYGP GGQGIINTTS HGIVVYYHYA NKNIGLAVDD
     YQFGWNTLTW TDGWPVVA
//