INUE_ASPNC
ID INUE_ASPNC Reviewed; 537 AA.
AC A2R0E0; Q0ZR33;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Extracellular exo-inulinase inuE;
DE EC=3.2.1.80;
DE Flags: Precursor;
GN Name=inuE; Synonyms=inu1; ORFNames=An12g08280;
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 [GENOMIC DNA], AND INDUCTION.
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17005986; DOI=10.1099/mic.0.29051-0;
RA Yuan X.L., Goosen C., Kools H., van der Maarel M.J.E.C.,
RA van den Hondel C.A.M.J.J., Dijkhuizen L., Ram A.F.J.;
RT "Database mining and transcriptional analysis of genes encoding inulin-
RT modifying enzymes of Aspergillus niger.";
RL Microbiology 152:3061-3073(2006).
RN [2]
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).
RN [3]
RP INDUCTION.
RX PubMed=17917744; DOI=10.1007/s00438-007-0290-5;
RA Yuan X.L., Roubos J.A., van den Hondel C.A., Ram A.F.;
RT "Identification of InuR, a new Zn(II)2Cys6 transcriptional activator
RT involved in the regulation of inulinolytic genes in Aspergillus niger.";
RL Mol. Genet. Genomics 279:11-26(2008).
RN [4]
RP INDUCTION.
RX PubMed=19166577; DOI=10.1186/1471-2164-10-44;
RA Jorgensen T.R., Goosen T., Hondel C.A., Ram A.F., Iversen J.J.;
RT "Transcriptomic comparison of Aspergillus niger growing on two different
RT sugars reveals coordinated regulation of the secretory pathway.";
RL BMC Genomics 10:44-44(2009).
CC -!- FUNCTION: Exo-inulinase involved in utilization of the plant storage
CC polymer inulin, consisting of fructooligosaccharides with a degree of
CC polymerization (DP) value from 2 to 60. Splits off terminal fructose
CC units successively from the non-reducing end of the inulin molecule,
CC and also hydrolyze sucrose and raffinose (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing (2->1)- and (2->6)-linked
CC beta-D-fructofuranose residues in fructans.; EC=3.2.1.80;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- INDUCTION: Expression is induced in presence of maltose, sucrose or
CC inulin and controlled by the catabolite repressor creA and by the
CC inulinolytic genes regulator inuR. {ECO:0000269|PubMed:17005986,
CC ECO:0000269|PubMed:17917744, ECO:0000269|PubMed:19166577}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR EMBL; DQ233222; ABB59682.1; -; Genomic_DNA.
DR EMBL; AM270284; CAK41278.1; -; Genomic_DNA.
DR RefSeq; XP_001395879.1; XM_001395842.1.
DR AlphaFoldDB; A2R0E0; -.
DR SMR; A2R0E0; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR CLAE; INU32C_ASPNG; -.
DR PaxDb; A2R0E0; -.
DR EnsemblFungi; CAK41278; CAK41278; An12g08280.
DR GeneID; 4986179; -.
DR KEGG; ang:ANI_1_2146104; -.
DR VEuPathDB; FungiDB:An12g08280; -.
DR HOGENOM; CLU_001528_3_0_1; -.
DR Proteomes; UP000006706; Chromosome 3L.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0051669; F:fructan beta-fructosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0051670; F:inulinase activity; IDA:AspGD.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001362; Glyco_hydro_32.
DR InterPro; IPR018053; Glyco_hydro_32_AS.
DR InterPro; IPR013189; Glyco_hydro_32_C.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE 2: Evidence at transcript level;
KW Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..537
FT /note="Extracellular exo-inulinase inuE"
FT /id="PRO_5000713588"
FT ACT_SITE 41
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT CARBOHYD 49
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 363
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 398
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 430
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 531
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 537 AA; 59150 MW; 7483D0530EA35671 CRC64;
MARLLKAVTV CALAGIAHAF NYDQPYRGQY HFSPQKNWMN DPNGLLYHNG TYHLFFQYNP
GGIEWGNISW GHATSEDLTH WEEQPVALLA RGYGSDVTEM YFSGSAVADV NNTSGFGKDG
KTPLVAMYTS YYPVAQTLPS GQTVQEDQQS QSIAYSLDDG LTWTTYDAAN PVIPNPPQPY
QAQYQNFRDP FVFWHDESQK WVVVTSIAEL HKLAIYTSDN LKDWKLVSEF GPYNAQGGVW
ECPGLFKLPL DGGSSTKWVI TSGLNPGGPP GTVGSGTQYF VGEFDGTTFT PDADTVYPGN
STANWMDWGP DFYAAAGYNG LSIKDHVHIG WMNNWQYGAN IPTYPWRSAM AIPRHLALKT
INNKTTLVQQ PQEAWSSISS KHPLYSRTYS TFSEGSTNAS TTGETFRVDL SFSATSKAST
FAIALRASAN FTEQTLAGYD FAKQQIFLDR TKSGDVSFDN TFASVYHGPL VPDSTSMVRL
SIFVDRSSVE VFGGQGETSL TAQIFPSNDA VHARLVSTGG ATEDVRVDVH NITSTWN
