ABNC_ASPNC
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 25-MAY-2022, entry version 69.
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 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 PaxDb; A5AAG2; -.
DR EnsemblFungi; CAK44404; CAK44404; An02g10550.
DR GeneID; 4979546; -.
DR KEGG; ang:ANI_1_1480024; -.
DR VEuPathDB; FungiDB:An02g10550; -.
DR HOGENOM; CLU_009397_5_0_1; -.
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 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..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
