INUE_ASPNG
ID INUE_ASPNG Reviewed; 537 AA.
AC Q76HP6;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Extracellular exo-inulinase inuE;
DE EC=3.2.1.80;
DE Flags: Precursor;
GN Name=inuE;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=12;
RX PubMed=16233531; DOI=10.1016/s1389-1723(03)90131-9;
RA Moriyama S., Tanaka H., Uwataki M., Muguruma M., Ohta K.;
RT "Molecular cloning and characterization of an exoinulinase gene from
RT Aspergillus niger strain 12 and its expression in Pichia pastoris.";
RL J. Biosci. Bioeng. 96:324-331(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=12;
RX PubMed=17502268; DOI=10.1263/jbb.103.293;
RA Moriyama S., Ohta K.;
RT "Functional characterization and evolutionary implication of the internal
RT 157-amino-acid sequence of an exoinulinase from Penicillium sp. strain TN-
RT 88.";
RL J. Biosci. Bioeng. 103:293-297(2007).
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:17502268}.
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:17502268};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3 mM for inulin {ECO:0000269|PubMed:17502268};
CC KM=111 mM for sucrose {ECO:0000269|PubMed:17502268};
CC pH dependence:
CC Optimum pH is 4.0. {ECO:0000269|PubMed:17502268};
CC Temperature dependence:
CC Optimum temperature is 60 degrees Celsius.
CC {ECO:0000269|PubMed:17502268};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:16233531}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR EMBL; AB100243; BAD01476.1; -; Genomic_DNA.
DR AlphaFoldDB; Q76HP6; -.
DR SMR; Q76HP6; -.
DR STRING; 5061.CADANGAP00010061; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR CLAE; INX32E_ASPNG; -.
DR VEuPathDB; FungiDB:An12g08280; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1183203; -.
DR VEuPathDB; FungiDB:ATCC64974_34960; -.
DR VEuPathDB; FungiDB:M747DRAFT_257211; -.
DR eggNOG; KOG0228; Eukaryota.
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_0000429405"
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
