INU1_KLUMA
ID INU1_KLUMA Reviewed; 555 AA.
AC P28999; Q9UWF4;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Inulinase;
DE EC=3.2.1.7;
DE AltName: Full=2,1-beta-D-fructanfructanohydrolase;
DE AltName: Full=Inulase;
DE Flags: Precursor;
GN Name=INU1; Synonyms=INU;
OS Kluyveromyces marxianus (Yeast) (Candida kefyr).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=4911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 24-56.
RC STRAIN=ATCC 12424 / NRRL Y-610;
RX PubMed=1840529; DOI=10.1016/0014-5793(91)80909-m;
RA Laloux O., Cassart J.-P., van Beeumen J., Delcour J., Vandenhaute J.;
RT "Cloning and sequencing of the inulinase gene of Kluyveromyces marxianus
RT var. marxianus ATCC 12424.";
RL FEBS Lett. 289:64-68(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26548 / CBS 6556 / NRRL Y-7571;
RX PubMed=7764385; DOI=10.1007/bf00170386;
RA Bergkamp R.J.M., Bootsman T.C., Toschka H.Y., Mooren A.T.A., Kox L.,
RA Verbakel J.M.A., Geerse R.H., Planta R.J.;
RT "Expression of an alpha-galactosidase gene under control of the homologous
RT inulinase promoter in Kluyveromyces marxianus.";
RL Appl. Microbiol. Biotechnol. 40:309-317(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 42265 / CBS 834 / NBRC 10287 / NRRL Y-329;
RA Zhang P.W., Tang N.Y., Zou Y., Huo K.K., Li Y.Y.;
RT "Cloning and sequence analysis of the major secretory protein gene from the
RT yeast Candida kefyr.";
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 24-43.
RC STRAIN=ATCC 26548 / CBS 6556 / NRRL Y-7571;
RX PubMed=2135869; DOI=10.1128/aem.56.11.3337-3345.1990;
RA Rouwenhorst R.J., Hensing M., Verbakel J., Scheffers W.A., van Dijken J.P.;
RT "Structure and properties of the extracellular inulinase of Kluyveromyces
RT marxianus CBS 6556.";
RL Appl. Environ. Microbiol. 56:3337-3345(1990).
CC -!- FUNCTION: Has both inulase and invertase activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (2->1)-beta-D-fructosidic linkages in
CC inulin.; EC=3.2.1.7;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR EMBL; X57202; CAA40488.1; -; Genomic_DNA.
DR EMBL; X68479; CAA48500.1; -; Genomic_DNA.
DR EMBL; AF135594; AAD27873.1; -; Genomic_DNA.
DR PIR; S17502; S17502.
DR PIR; S31330; S31330.
DR AlphaFoldDB; P28999; -.
DR SMR; P28999; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR CLAE; INU32A_KLUMA; -.
DR BRENDA; 3.2.1.26; 1120.
DR BRENDA; 3.2.1.7; 1120.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0051670; F:inulinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 Cleavage on pair of basic residues; Direct protein sequencing;
KW Glycoprotein; Glycosidase; Hydrolase; Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT PROPEP 17..23
FT /evidence="ECO:0000255"
FT /id="PRO_0000033408"
FT CHAIN 24..555
FT /note="Inulinase"
FT /id="PRO_0000033409"
FT ACT_SITE 53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 50..53
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 113..114
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 181..182
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 334
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 176
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 226
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 255
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 385
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 549
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 3
FT /note="F -> L (in strain: CBS 6556)"
FT VARIANT 165
FT /note="E -> Q (in strain: CBS 6556)"
FT VARIANT 168
FT /note="T -> S (in strain: CBS 6556)"
FT VARIANT 251
FT /note="V -> A (in strain: CBS 6556)"
FT VARIANT 252
FT /note="D -> DS (in strain: CBS 6556)"
FT VARIANT 299
FT /note="G -> D (in strain: CBS 6556)"
FT VARIANT 393
FT /note="N -> I (in strain: CBS 834)"
FT VARIANT 479
FT /note="T -> N (in strain: CBS 6556)"
FT CONFLICT 24
FT /note="D -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="H -> Y (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 555 AA; 62214 MW; 723BAADDC3BF0907 CRC64;
MKFAYSLLLP LAGVSASVIN YKRDGDSKAI TNTTFSLNRP SVHFTPSHGW MNDPNGLWYD
AKEEDWHLYY QYNPAATIWG TPLYWGHAVS KDLTSWTDYG ASLGPGSDDA GAFSGSMVID
YNNTSGFFNS SVDPRQRAVA VWTLSKGPSQ AQHISYSLDG GYTFEHYTDN AVLDINSSNF
RDPKVFWHEG ENGEDGRWIM AVAESQVFSV LFYSSPNLKN WTLESNFTHH GWTGTQYECP
GLVKVPYDSV VDSSNSSDSK PDSAWVLFVS INPGGPLGGS VTQYFVGDFN GTHFTPIDGQ
TRFLDMGKDY YALQTFFNTP NEKDVYGIAW ASNWQYAQQA PTDPWRSSMS LVRQFTLKDF
STNPNSADVV LNSQPVLNYD ALRKNGTTYS ITNYTVTSEN GKKIKLDNPS GSLEFHLEYV
FNGSPDIKSN VFADLSLYFK GNNDDNEYLR LGYETNGGAF FLDRGHTKIP FVKENLFFTH
QLAVTNPVSN YTTNVFDVYG VIDKNIIELY FDNGNVVSTN TFFFSTNNVI GEIDIKSPYD
KAYTINSFNV TQFNV
