INV_KLULA
ID INV_KLULA Reviewed; 609 AA.
AC Q9Y746; Q6CX83;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 109.
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; OrderedLocusNames=KLLA0A10417g;
OS Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX NCBI_TaxID=284590;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=10394924; DOI=10.1007/s004380050030;
RA Georis I., Cassart J.-P., Breunig K.D., Vandenhaute J.;
RT "Glucose repression of the Kluyveromyces lactis invertase gene KIINV1 does
RT not require Mig1p.";
RL Mol. Gen. Genet. 261:862-870(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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; AF079370; AAD29850.1; -; Genomic_DNA.
DR EMBL; CR382121; CAH03044.1; -; Genomic_DNA.
DR RefSeq; XP_451456.1; XM_451456.1.
DR AlphaFoldDB; Q9Y746; -.
DR SMR; Q9Y746; -.
DR STRING; 28985.XP_451456.1; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PRIDE; Q9Y746; -.
DR EnsemblFungi; CAH03044; CAH03044; KLLA0_A10417g.
DR GeneID; 2896726; -.
DR KEGG; kla:KLLA0_A10417g; -.
DR eggNOG; KOG0228; Eukaryota.
DR HOGENOM; CLU_001528_3_3_1; -.
DR InParanoid; Q9Y746; -.
DR OMA; GTEWRHA; -.
DR Proteomes; UP000000598; Chromosome A.
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; Reference proteome; Signal.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..609
FT /note="Invertase"
FT /id="PRO_0000033396"
FT ACT_SITE 59
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 56..59
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 119..120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 187..188
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 389
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 32
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 36
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 128
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 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 284
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 345
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 420
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 440
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 448
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 477
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 545
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 609 AA; 68349 MW; 8C1F4F19D75B6319 CRC64;
MLKLLSLMVP LASAAVIHRR DANISAIASE WNSTSNSSSS LSLNRPAVHY SPEEGWMNDP
NGLWYDAKEE DWHIYYQYYP DAPHWGLPLT WGHAVSKDLT VWDEQGVAFG PEFETAGAFS
GSMVIDYNNT SGFFNSSTDP RQRVVAIWTL DYSGSETQQL SYSHDGGYTF TEYSDNPVLD
IDSDAFRDPK VFWYQGEDSE SEGNWVMTVA EADRFSVLIY SSPDLKNWTL ESNFSREGYL
GYNYECPGLV KVPYVKNTTY ASAPGSNITS SGPLHPNSTV SFSNSSSIAW NASSVPLNIT
LSNSTLVDET SQLEEVGYAW VMIVSFNPGS ILGGSGTEYF IGDFNGTHFE PLDKQTRFLD
LGKDYYALQT FFNTPNEVDV LGIAWASNWQ YANQVPTDPW RSSMSLVRNF TITEYNINSN
TTALVLNSQP VLDFTSLRKN GTSYTLENLT LNSSSHEVLE FEDPTGVFEF SLEYSVNFTG
IHNWVFTDLS LYFQGDKDSD EYLRLGYEAN SKQFFLDRGH SNIPFVQENP FFTQRLSVSN
PPSSNSSTFD VYGIVDRNII ELYFNNGTVT STNTFFFSTG NNIGSIIVKS GVDDVYEIES
LKVNQFYVD
