ID   SCRB_PEDPE              Reviewed;         501 AA.
AC   P43471;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   04-NOV-2026, entry version 96.
DE   RecName: Full=Sucrose-6-phosphate hydrolase;
DE            Short=Sucrase;
DE            EC=3.2.1.26;
DE   AltName: Full=Invertase;
GN   Name=scrB;
OS   Pediococcus pentosaceus.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=1255;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PPE1.0;
RA   Leenhouts K.K.J., Bolhuis A.A., Kok J.J., Venema G.G.;
RT   "The sucrose and raffinose operons of Pediococcus pentosaceus PPE1.0.";
RL   Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   IDENTIFICATION OF FRAMESHIFTS.
RX   PubMed=11234378;
RA   Naumoff D.G., Livshits V.A.;
RT   "Molecular structure of the Lactobacillus plantarum sucrose utilization
RT   locus: comparison with Pediococcus pentosaceus.";
RL   Mol. Biol. (Mosk.) 35:19-27(2001).
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   -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA25568.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA83669.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; Z32771; CAA83669.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; L32093; AAA25568.1; ALT_FRAME; Genomic_DNA.
DR   PIR; S44258; S44258.
DR   RefSeq; WP_011673113.1; NZ_CAKMAM010000006.1.
DR   AlphaFoldDB; P43471; -.
DR   SMR; P43471; -.
DR   GeneID; 33062844; -.
DR   OMA; AAFEMIC; -.
DR   UniPathway; UPA00238; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004564; F:beta-fructofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005985; P:sucrose metabolic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd18623; GH32_ScrB-like; 1.
DR   Gene3D; 2.60.120.560; Exo-inulinase, domain 1; 1.
DR   Gene3D; 2.115.10.20; Glycosyl hydrolase domain, family 43; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR051214; GH32_Enzymes.
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   InterPro; IPR006232; Suc6P_hydrolase.
DR   NCBIfam; TIGR01322; scrB_fam; 1.
DR   PANTHER; PTHR43101; BETA-FRUCTOSIDASE; 1.
DR   PANTHER; PTHR43101:SF1; BETA-FRUCTOSIDASE; 1.
DR   Pfam; PF08244; Glyco_hydro_32C; 1.
DR   Pfam; PF00251; Glyco_hydro_32N; 1.
DR   SMART; SM00640; Glyco_32; 1.
DR   SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Glycosidase; Hydrolase.
FT   CHAIN           1..501
FT                   /note="Sucrose-6-phosphate hydrolase"
FT                   /id="PRO_0000169874"
FT   ACT_SITE        47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   BINDING         44..47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         106..107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         167..168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   501 AA;  56690 MW;  7D1337951DFAFA21 CRC64;
     MIWNRKTRYT PYEQWPATKL PQLVAQARQS KWRMQHHIQP TSGLLNDPNG FSYFDGQWHL
     FYQVFPFGPV HGLKSWQHVT SKNLVDWHDE GLAIRPDTPY DSHGAYTGTA LPIDDQLFIM
     YTGNVRTADW QRESYQLGAW MDTDNHIKKL SRPLIAHAPA GYTSSFRDPD LIRNDHGYYA
     LIGAQTTTEI GAILVYFSKD LTTWTCQGEL NVPANARGYM IECPNLVWID QQPVLLFCPQ
     GLSQATIPYQ NIYPNMYLVA DQLNLAQAQF TEPHALTQLD DGFDVYATQA INAPDGRALA
     VSWIGLPEIS YPTDRENWAH CLSLVKELTL KDGHLYQNPV AAVDDLRTTA HDLVFEQQRA
     TVAALNGSFE LLLTVPADKT VTVNIADQQE SGQLQVTVDA NHGQVMIDRR HTGNSFAEDY
     GQTRQVELTA HKTIKIRLII DVSVFECYID NGYSVMTGRF FLNATPSRLN VQGDTTAVTG
     KVWEWRQSEH TGVDNNETKI K
//