INV1_SCHPO
ID INV1_SCHPO Reviewed; 581 AA.
AC O59852; P78891;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Invertase;
DE EC=3.2.1.26;
DE AltName: Full=Beta-fructofuranosidase;
DE AltName: Full=Saccharase;
DE Flags: Precursor;
GN Name=inv1; ORFNames=SPCC191.11;
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 [GENOMIC DNA].
RX PubMed=9535817; DOI=10.1006/bbrc.1998.8406;
RA Tanaka N., Ohuchi N., Mukai Y., Osaka Y., Ohtani Y., Tabuchi M.,
RA Bhuiyan M.S.A., Fukui H., Harashima S., Takegawa K.;
RT "Isolation and characterization of an invertase and its repressor genes
RT from Schizosaccharomyces pombe.";
RL Biochem. Biophys. Res. Commun. 245:246-253(1998).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 88-581.
RC STRAIN=PR745;
RX PubMed=9501991; DOI=10.1093/dnares/4.6.363;
RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.;
RT "Identification of open reading frames in Schizosaccharomyces pombe
RT cDNAs.";
RL DNA Res. 4:363-369(1997).
RN [4]
RP GLYCOSYLATION AT ASN-37; ASN-40; ASN-46; ASN-57; ASN-62; ASN-79; ASN-168;
RP ASN-175; ASN-322; ASN-399; ASN-409; ASN-425; ASN-446; ASN-452; ASN-519 AND
RP ASN-569.
RX PubMed=2187435; DOI=10.1042/bj2670697;
RA Moreno S., Sanchez Y., Rodriguez L.;
RT "Purification and characterization of the invertase from
RT Schizosaccharomyces pombe.";
RL Biochem. J. 267:697-702(1990).
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 -!- PTM: Glycosylated; contains 67% carbohydrates. This is composed of
CC equimolar amounts of mannose and galactose. There is also a small
CC amount of glucosamine present. {ECO:0000269|PubMed:2187435}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB011433; BAA25684.1; -; Genomic_DNA.
DR EMBL; CU329672; CAB41057.1; -; Genomic_DNA.
DR EMBL; D89242; BAA13903.1; -; mRNA.
DR PIR; JE0102; JE0102.
DR RefSeq; NP_588300.1; NM_001023290.2.
DR AlphaFoldDB; O59852; -.
DR SMR; O59852; -.
DR BioGRID; 275797; 7.
DR STRING; 4896.SPCC191.11.1; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR CLAE; SUC32A_SCHPO; -.
DR iPTMnet; O59852; -.
DR MaxQB; O59852; -.
DR PaxDb; O59852; -.
DR EnsemblFungi; SPCC191.11.1; SPCC191.11.1:pep; SPCC191.11.
DR GeneID; 2539227; -.
DR KEGG; spo:SPCC191.11; -.
DR PomBase; SPCC191.11; inv1.
DR VEuPathDB; FungiDB:SPCC191.11; -.
DR eggNOG; KOG0228; Eukaryota.
DR HOGENOM; CLU_001528_3_3_1; -.
DR InParanoid; O59852; -.
DR OMA; YPDEHEN; -.
DR PhylomeDB; O59852; -.
DR PRO; PR:O59852; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; ISS:PomBase.
DR GO; GO:0004564; F:beta-fructofuranosidase activity; IMP:PomBase.
DR GO; GO:0004575; F:sucrose alpha-glucosidase activity; IDA:PomBase.
DR GO; GO:0005987; P:sucrose catabolic process; IMP: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 1: Evidence at protein level;
KW Glycoprotein; Glycosidase; Hydrolase; Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..581
FT /note="Invertase"
FT /id="PRO_0000033397"
FT ACT_SITE 97
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 94..97
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 158..159
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 227..228
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 37
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:2187435"
FT CARBOHYD 40
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:2187435"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:2187435"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:2187435"
FT CARBOHYD 62
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:2187435"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:2187435"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:2187435"
FT CARBOHYD 175
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:2187435"
FT CARBOHYD 322
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:2187435"
FT CARBOHYD 399
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:2187435"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:2187435"
FT CARBOHYD 425
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:2187435"
FT CARBOHYD 446
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:2187435"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:2187435"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:2187435"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:2187435"
FT CONFLICT 186..189
FT /note="Missing (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="H -> Y (in Ref. 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="A -> P (in Ref. 3; BAA13903)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="Q -> L (in Ref. 3; BAA13903)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="D -> N (in Ref. 3; BAA13903)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="I -> M (in Ref. 3; BAA13903)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="M -> L (in Ref. 3; BAA13903)"
FT /evidence="ECO:0000305"
FT CONFLICT 256
FT /note="S -> P (in Ref. 3; BAA13903)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 581 AA; 64407 MW; 70206A6CD1F27EC4 CRC64;
MFLKYILASG ICLVSLLSST NAAPRHLYVK RYPVIYNASN ITEVSNSTTV PPPPFVNTTA
PNGTCLGNYN EYLPSGYYNA TDRPKIHFTP SSGFMNDPNG LVYTGGVYHM FFQYSPKTLT
AGEVHWGHTV SKDLIHWENY PIAIYPDEHE NGVLSLPFSG SAVVDVHNSS GLFSNDTIPE
ERIVLIYTDH WTGVAERQAI AYTTDGGYTF KKYSGNPVLD INSLQFRDPK VIWDFDANRW
VMIVAMSQNY GIAFYSSYDL IHWTELSVFS TSGYLGLQYE CPGMARVPVE GTDEYKWVLF
ISINPGAPLG GSVVQYFVGD WNGTNFVPDD GQTRFVDLGK DFYASALYHS SSANADVIGV
GWASNWQYTN QAPTQVFRSA MTVARKFTLR DVPQNPMTNL TSLIQTPLNV SLLRDETLFT
APVINSSSSL SGSPITLPSN TAFEFNVTLS INYTEGCTTG YCLGRIIIDS DDPYRLQSIS
VDVDFAASTL VINRAKAQMG WFNSLFTPSF ANDIYIYGNV TLYGIVDNGL LELYVNNGEK
TYTNDFFFLQ GATPGQISFA AFQGVSFNNV TVTPLKTIWN C
