ID   INVX_SCHPO              Reviewed;         508 AA.
AC   O42878; Q9P4X5;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   22-FEB-2012, sequence version 3.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Putative invertase;
DE            EC=3.2.1.26;
DE   AltName: Full=Beta-fructofuranosidase;
DE   AltName: Full=Saccharase;
GN   ORFNames=SPAC8E11.01c, SPAC959.01;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR   EMBL; CU329670; CAA17022.2; -; Genomic_DNA.
DR   PIR; T39155; T39155.
DR   RefSeq; NP_594168.2; NM_001019592.2.
DR   AlphaFoldDB; O42878; -.
DR   SMR; O42878; -.
DR   BioGRID; 279155; 8.
DR   STRING; 4896.SPAC8E11.01c.1; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   MaxQB; O42878; -.
DR   PaxDb; O42878; -.
DR   EnsemblFungi; SPAC8E11.01c.1; SPAC8E11.01c.1:pep; SPAC8E11.01c.
DR   GeneID; 2542702; -.
DR   KEGG; spo:SPAC8E11.01c; -.
DR   PomBase; SPAC8E11.01c; -.
DR   VEuPathDB; FungiDB:SPAC8E11.01c; -.
DR   eggNOG; KOG0228; Eukaryota.
DR   HOGENOM; CLU_001528_3_3_1; -.
DR   InParanoid; O42878; -.
DR   PRO; PR:O42878; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; HDA:PomBase.
DR   GO; GO:0004575; F:sucrose alpha-glucosidase activity; ISO:PomBase.
DR   GO; GO:0005987; P:sucrose catabolic process; ISO:PomBase.
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   Cytoplasm; Glycosidase; Hydrolase; Nucleus; Reference proteome.
FT   CHAIN           1..508
FT                   /note="Putative invertase"
FT                   /id="PRO_0000169868"
FT   ACT_SITE        18
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   BINDING         15..18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         34
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         75..76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         149..150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   508 AA;  58054 MW;  BC81B3F546294734 CRC64;
     MPVRPCIHFT PPEGFMNDPN GLVYSNGKWH LFFQWNPTGN QAGNQHWGHA VSKNLYKWKL
     LPTALAPGDD HGLMFSGSAV IDKTNSSGFF ESGFFSRKSV DPEERIVLIY TTHYDNRETQ
     NIAYSLDGGI TFIKYKKNPI LDIKESQFRD PKVFWHEESR AWIMVVVLAQ KYKVLFYHSL
     NLRDWVKLSE FGSAGVLGYQ YECPDFVRLP IEGTDEFRWV LIVSINPGSS INGGSMVQYF
     IGDFDGQTFT PIDSASRILD CGHDCYATQT FGNAPDGRVI SISWASNWNY TNDVPMRMKH
     RGMFTIPREL TLCYTHLNQE TRGLVLRQRP VNLHHLYYPD SLPAPLLLNR VCEFPTVWTS
     ATVFYLAVSI PKSIVLESPM EFLCLTWSTT PDVETSKEYF ELGYRFHDGA VYVERGVCSS
     SWKYPLYPER CTSSVPPSSY EDNYILEIEA VVDHSIIEVY LQGGIMCLTN AYYFKGDEPL
     QYYYLRVPTG ASLAKSGMQP LLNNRPHS