INU2_ASPFI
ID INU2_ASPFI Reviewed; 516 AA.
AC O94220;
DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Extracellular endo-inulinase inu2;
DE EC=3.2.1.7;
DE AltName: Full=2,1-beta-D-fructanfructanohydrolase;
DE AltName: Full=Inulase;
DE Flags: Precursor;
GN Name=inu2;
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].
RC STRAIN=ATCC 16882 / CBS 555.65 / NRRL 364;
RA Uhm T., Chae S., Lee D., Kim S., Cassart J.-P., Vandenhaute J.;
RT "Cloning and nucleotide sequence of the endoinulinase-encoding gene, inu2,
RT from Aspergillus ficuum.";
RL Biotechnol. Lett. 20:809-812(1998).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF
RP MET-41; ASN-42; GLU-43; GLN-59; PRO-62; TRP-67; ILE-70; PHE-99; ARG-175;
RP ASN-265; ARG-295 AND ASP-298.
RX PubMed=24251113; DOI=10.1016/j.fob.2013.10.009;
RA Vandamme A.M., Michaux C., Mayard A., Housen I.;
RT "Asparagine 42 of the conserved endo-inulinase INU2 motif WMNDPN from
RT Aspergillus ficuum plays a role in activity specificity.";
RL FEBS Open Bio 3:467-472(2013).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE,
RP GLYCOSYLATION AT ASN-372, AND CATALYTIC ACTIVITY.
RX PubMed=22750808; DOI=10.1016/j.biochi.2012.06.020;
RA Pouyez J., Mayard A., Vandamme A.M., Roussel G., Perpete E.A., Wouters J.,
RA Housen I., Michaux C.;
RT "First crystal structure of an endo-inulinase, INU2, from Aspergillus
RT ficuum: discovery of an extra-pocket in the catalytic domain responsible
RT for its endo-activity.";
RL Biochimie 94:2423-2430(2012).
CC -!- FUNCTION: Endo-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. {ECO:0000269|PubMed:24251113}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (2->1)-beta-D-fructosidic linkages in
CC inulin.; EC=3.2.1.7; Evidence={ECO:0000269|PubMed:22750808,
CC ECO:0000269|PubMed:24251113};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24251113}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR EMBL; AJ006951; CAA07345.1; -; Genomic_DNA.
DR PDB; 3RWK; X-ray; 2.10 A; X=1-516.
DR PDB; 3SC7; X-ray; 1.50 A; X=1-516.
DR PDBsum; 3RWK; -.
DR PDBsum; 3SC7; -.
DR AlphaFoldDB; O94220; -.
DR SMR; O94220; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR CLAE; INU32B_ASPFI; -.
DR iPTMnet; O94220; -.
DR BRENDA; 3.2.1.7; 503.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0051670; F:inulinase 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; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glycoprotein; Glycosidase;
KW Hydrolase; Polysaccharide degradation; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..516
FT /note="Extracellular endo-inulinase inu2"
FT /id="PRO_0000033410"
FT ACT_SITE 43
FT /evidence="ECO:0000250"
FT BINDING 41..43
FT /ligand="substrate"
FT BINDING 61
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22750808"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22750808"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22750808"
FT CARBOHYD 108
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 210
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 372
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:22750808"
FT MUTAGEN 41
FT /note="M->A: Decreases catalytic activity."
FT /evidence="ECO:0000269|PubMed:24251113"
FT MUTAGEN 42
FT /note="N->G: Strongly decreases catalytic activity."
FT /evidence="ECO:0000269|PubMed:24251113"
FT MUTAGEN 43
FT /note="E->D: Strongly decreases catalytic activity."
FT /evidence="ECO:0000269|PubMed:24251113"
FT MUTAGEN 59
FT /note="Q->A: Impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:24251113"
FT MUTAGEN 62
FT /note="P->G: Impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:24251113"
FT MUTAGEN 67
FT /note="W->A: Impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:24251113"
FT MUTAGEN 70
FT /note="I->A: Decreases catalytic activity."
FT /evidence="ECO:0000269|PubMed:24251113"
FT MUTAGEN 99
FT /note="F->A: Strongly decreases catalytic activity."
FT /evidence="ECO:0000269|PubMed:24251113"
FT MUTAGEN 175
FT /note="R->A: Impairs catalytic activity."
FT /evidence="ECO:0000269|PubMed:24251113"
FT MUTAGEN 265
FT /note="N->A: Decreases catalytic activity."
FT /evidence="ECO:0000269|PubMed:24251113"
FT MUTAGEN 295
FT /note="R->A: Decreases catalytic activity."
FT /evidence="ECO:0000269|PubMed:24251113"
FT MUTAGEN 298
FT /note="D->A: Decreases catalytic activity."
FT /evidence="ECO:0000269|PubMed:24251113"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 37..50
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 53..61
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 71..82
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 96..105
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 121..129
FT /evidence="ECO:0007829|PDB:3SC7"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 135..144
FT /evidence="ECO:0007829|PDB:3SC7"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:3SC7"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 170..173
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:3SC7"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 187..193
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 199..210
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 212..218
FT /evidence="ECO:0007829|PDB:3SC7"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 243..246
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 268..274
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:3SC7"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:3SC7"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 329..332
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 339..346
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 349..356
FT /evidence="ECO:0007829|PDB:3SC7"
FT HELIX 358..363
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 364..375
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 388..398
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 403..410
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 416..421
FT /evidence="ECO:0007829|PDB:3SC7"
FT TURN 422..425
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 443..450
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 459..466
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 469..474
FT /evidence="ECO:0007829|PDB:3SC7"
FT TURN 475..478
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 479..484
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 493..501
FT /evidence="ECO:0007829|PDB:3SC7"
FT STRAND 503..513
FT /evidence="ECO:0007829|PDB:3SC7"
SQ SEQUENCE 516 AA; 55793 MW; 44ED9D44B465593F CRC64;
MLNPKVAYMV WMTCLGLTLP SQAQSNDYRP SYHFTPDQYW MNEPNGLIKI GSTWHLFFQH
NPTANVWGNI CWGHATSTDL MHWAHKPTAI ADENGVEAFT GTAYYDPNNT SGLGDSANPP
YLAWFTGYTT SSQTQDQRLA FSVDNGATWT KFQGNPIIST SQEAPHDITG GLESRDPKVF
FHRQSGNWIM VLAHGGQDKL SFWTSADTIN WTWQSDLKST SINGLSSDIT GWEVPDMFEL
PVEGTEETTW VVMMTPAEGS PAGGNGVLAI TGSFDGKSFT ADPVDASTMW LDNGRDFDGA
LSWVNVPASD GRRIIAAVMN SYGSNPPTTT WKGMLSFPRT LSLKKVGTQQ HFVQQPITEL
DTISTSLQIL ANQTITPGQT LLSSIRGTAL DVRVAFYPDA GSVLSLAVRK GASEQTVIKY
TQSDATLSVD RTESGDISYD PAAGGVHTAK LEEDGTGLVS IRVLVDTCSV EVFGGQGEAV
ISDLIFPSDS SDGLALEVTG GNAVLQSVDV RSVSLE
