INV4_YEASX
ID INV4_YEASX Reviewed; 532 AA.
AC P10596;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Invertase 4;
DE EC=3.2.1.26;
DE AltName: Full=Beta-fructofuranosidase 4;
DE AltName: Full=Saccharase;
DE Flags: Precursor;
GN Name=SUC4;
OS Saccharomyces cerevisiae (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=4932;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-73.
RX PubMed=2835632; DOI=10.1007/bf00425699;
RA Hohmann S., Gozalbo D.;
RT "Structural analysis of the 5' regions of yeast SUC genes revealed
RT analogous palindromes in SUC, MAL and GAL.";
RL Mol. Gen. Genet. 211:446-454(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Hohmann S.;
RL Submitted (NOV-1988) to the EMBL/GenBank/DDBJ databases.
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; X07572; CAA30459.1; -; Genomic_DNA.
DR PIR; S27373; S27373.
DR AlphaFoldDB; P10596; -.
DR SMR; P10596; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR SGD; S000029533; SUC4.
DR VEuPathDB; FungiDB:YIL162W; -.
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..19
FT CHAIN 20..532
FT /note="Invertase 4"
FT /id="PRO_0000033402"
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 102..103
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 311
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
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 165
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 356
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
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 512
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 532 AA; 60575 MW; A56EA2E3A49125EB CRC64;
MLLQAFIFLL AGFAAKISAL MTNETSDRPL VHFTPNKGWM NDPNGLWYDA KEGKWHLYFQ
YNPNDTVWGL PLFWGHATSN DLTHWQDEPV AIAPKRNDSG AYSGSMVIDH NNTSEFFNDT
VDPRQRCVAI WTYNTPESEE QYISYSLDGG YTFTEYQKNP VLAANSTQFR DPKVFWYEPS
QKWIMTAAKS QDYKIEIYSS DDLKSWKLES AFANEGFLGY QYECPGLIEV PTEQDPSKSH
WVMFISINPG APAGGSFNQY FVGSFNGTHF EAYDNQSRVV DFGKDYYALQ TFFNTDPTYG
SALGIAWASN WEYSAFVPTN PWRSSMSLVR KFSLNTEYQA NPETELINLK AEPILNISNA
GPWLHFASNS TLTKANSFSV DLSNSTGTLE FELVYAVNTT QSVSKSVFSD LSLWFKGLED
PEEYLRMGFE ASASSFFLDR GNSKVKFVKE NPYFTNRMSV NNQPFKSEND LSYYKVYGLL
DQNILELYFN DGDVVSTNTY FMTTGNALGS VNMTTGVDNL FYIDKFQVRE VK
