INV_DEBHA
ID INV_DEBHA Reviewed; 534 AA.
AC Q6BJW6;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Invertase;
DE EC=3.2.1.26;
DE AltName: Full=Beta-fructofuranosidase;
DE AltName: Full=Saccharase;
DE Flags: Precursor;
GN Name=INV; OrderedLocusNames=DEHA2F26818g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382138; CAG89931.2; -; Genomic_DNA.
DR RefSeq; XP_461505.2; XM_461505.1.
DR AlphaFoldDB; Q6BJW6; -.
DR SMR; Q6BJW6; -.
DR STRING; 4959.XP_461505.2; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR EnsemblFungi; CAG89931; CAG89931; DEHA2F26818g.
DR GeneID; 2903733; -.
DR KEGG; dha:DEHA2F26818g; -.
DR VEuPathDB; FungiDB:DEHA2F26818g; -.
DR eggNOG; KOG0228; Eukaryota.
DR HOGENOM; CLU_001528_3_3_1; -.
DR InParanoid; Q6BJW6; -.
DR OMA; GTEWRHA; -.
DR OrthoDB; 405663at2759; -.
DR Proteomes; UP000000599; Chromosome F.
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..21
FT /evidence="ECO:0000255"
FT CHAIN 22..534
FT /note="Invertase"
FT /id="PRO_0000033393"
FT ACT_SITE 49
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT BINDING 46..49
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 67
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 109..110
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 177..178
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 313
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
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 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 218
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 392
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 534 AA; 60991 MW; 5EFBA6841CAC6005 CRC64;
MKITTLVASI LMSVLLEPVI ASFIDTGKDT SAYNRPLIHL TPNVGWLNDP NGLFYDKKTS
VWHAYYQYNP NDTIWGQPLY WGHSSSKDLT HWEEHQVALG PQNDDEGIFS GSIVIDYNNT
SGFFDESIDK DQRVVAIYTN SIPDTQTQDI AYSLDGGETF TKYKKNPVID VNSTQFRDPK
VFWHEETNKW IMVVSKSQEY KIQIFGSLDL KTWDLHSNFT SGYLGNQYEC PGLIKVPIEN
TNDYKWVMFL AINPGSPAGG SSNQYFIGEF DGFEFKQDDS ITRVMDAGKD FYAFQTFSDN
EQDVIGLAWA SNWQYANVVP TNPWRSSMSL ARKYTLGYVN QNVETKIMTL IQTPILNNLD
VINKVEKNNH LLTKNDSVIT NFSSSTGLLD FNTTFKVVGE SIDSNSLSNI EILIHSQMSN
SSTESIKVGF DRSVSAFYFN RDIPNVEFNN NPYFTNKFST YVEPSHYDED DMPVYKIYGI
VDKNILELYF NDGTQTMTNT FFMSEDKYPH QIEIASNVDG QFELQSLLIR ELNN
