ID   INUE_ASPFI              Reviewed;         537 AA.
AC   E1ABX2;
DT   11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 1.
DT   03-AUG-2022, entry version 36.
DE   RecName: Full=Extracellular exo-inulinase inuE;
DE            EC=3.2.1.80;
DE   Flags: Precursor;
GN   Name=exoI;
OS   Aspergillus ficuum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5058;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX   PubMed=23399248; DOI=10.1016/j.carbpol.2012.11.087;
RA   Chen X.M., Xu X.M., Jin Z.Y., Chen H.Q.;
RT   "Expression of an exoinulinase gene from Aspergillus ficuum in Escherichia
RT   coli and its characterization.";
RL   Carbohydr. Polym. 92:1984-1990(2013).
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.
CC       {ECO:0000269|PubMed:23399248}.
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         Evidence={ECO:0000269|PubMed:23399248};
CC   -!- ACTIVITY REGULATION: The catalytic activity is increased by manganese
CC       cathions, but strongly inhibited by other metal ions such as cupper,
CC       aluminum, silver, iron, nickel, zinc and magnesium cathions.
CC       {ECO:0000269|PubMed:23399248}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=7.1 mM for inulin {ECO:0000269|PubMed:23399248};
CC         KM=347 mM for sucrose {ECO:0000269|PubMed:23399248};
CC         Vmax=1 mmol/min/mg enzyme toward inulin
CC         {ECO:0000269|PubMed:23399248};
CC         Vmax=12 mmol/min/mg enzyme toward sucrose
CC         {ECO:0000269|PubMed:23399248};
CC       pH dependence:
CC         Optimum pH is 4.0 when inulin is a substrate and 5.0 when sucrose is
CC         a substrate. {ECO:0000269|PubMed:23399248};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius when inulin is a substrate
CC         and 55 degrees Celsius when sucrose is a substrate.
CC         {ECO:0000269|PubMed:23399248};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 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; HM587130; ADM21204.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1ABX2; -.
DR   SMR; E1ABX2; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   CLAE; INX32A_ASPFI; -.
DR   PRIDE; E1ABX2; -.
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: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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Glycoprotein; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..537
FT                   /note="Extracellular exo-inulinase inuE"
FT                   /id="PRO_0000429404"
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;  59143 MW;  940BF99CB2278D6D CRC64;
     MARLLKAVTV CALAGIAHAF NYDQPYRGQY HFSPQKNWMN DPNGLLYHNG TYHLFFQYNP
     GGIEWGNISW GHATSEDLTH WEEQPVALLA RGYGSDVTEM YFSGSAVADV NNTSGFGKDG
     KTPLVAMYTS YYPVAQTLPS GQTVQEDQQS QSIAYSLDDG LTWTTYDAAN PVIPNPPQPY
     QAQYQNFRDP FVFWHDESHK 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 VPDSTGMVRL
     SIFVDRSSVE VFGGQGETTL TAQIFPSNDA VHARLVSTGG ATEDVRVDVH NITSTWN