ID   INV1_WICAO              Reviewed;         550 AA.
AC   P40912;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Invertase;
DE            EC=3.2.1.26;
DE   AltName: Full=Beta-fructofuranosidase 2;
DE   AltName: Full=Saccharase;
DE   Flags: Precursor;
GN   Name=INV1;
OS   Wickerhamomyces anomalus (Yeast) (Hansenula anomala).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Phaffomycetaceae; Wickerhamomyces.
OX   NCBI_TaxID=4927;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8595669; DOI=10.1007/bf02221553;
RA   Perez J.A., Rodriguez J., Rodriguez L., Ruiz T.;
RT   "Cloning and sequence analysis of the invertase gene INV 1 from the yeast
RT   Pichia anomala.";
RL   Curr. Genet. 29:234-240(1996).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing beta-D-fructofuranoside
CC         residues in beta-D-fructofuranosides.; EC=3.2.1.26;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10067};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR   EMBL; X80640; CAA56684.1; -; Genomic_DNA.
DR   PIR; S65753; S65753.
DR   AlphaFoldDB; P40912; -.
DR   SMR; P40912; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   CLAE; SUC32A_HANAN; -.
DR   BRENDA; 3.2.1.26; 1135.
DR   GO; GO:0004564; F:beta-fructofuranosidase 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   3: Inferred from homology;
KW   Glycoprotein; Glycosidase; Hydrolase; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..550
FT                   /note="Invertase"
FT                   /id="PRO_0000033395"
FT   ACT_SITE        42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   BINDING         39..42
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         103..104
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         170..171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         313
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        112
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        211
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        237
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        333
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        364
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        420
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   550 AA;  63188 MW;  192BCD722455E121 CRC64;
     MIQLSPLLLL PLFSVFNSIA DASTEYLRPQ IHLTPDQGWM NDPNGMFYDR KDKLWHVYFQ
     HNPDKKSIWA TPVTWGHSTS KDLLTWDYHG NALEPENDDE GIFSGSVVVD RNNTSGFFND
     STDPEQRIVA IYTNNAQLQT QEIAYSLDKG YSFIKYDQNP VINVNSSQQR DPKVLWHDES
     NQWIMVVAKT QEFKVQIYGS PDLKKWDLKS NFTSNGYLGF QYECPGLFKL PIENPLNDTV
     TSKWVLLLAI NPGSPLGGSI NEYFIGDFDG TTFHPDDGAT RFMDIGKDFY AFQSFDNTEP
     EDGALGLAWA SNWQYANTVP TENWRSSMSL VRNYTLKYVD VNPENYGLTL IQKPVYDTKE
     TRLNETLKTL ETINEYEVND LKLDKSSFVA TDFNTERNAT GVFEFDLKFT QTDLKMGYSN
     MTTQFGLYIH SQTVKGSQET LQLVFDTLST TWYIDRTTQH SFQRNSPVFT ERISTYVEKI
     DTTDQGNVYT LYGVVDRNIL ELYFNDGSIA MTNTFFFREG KIPTSFEVVC DSEKSFITID
     ELSVRELARK