ID   SCRB_STAXY              Reviewed;         494 AA.
AC   Q05936;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   02-SEP-2026, entry version 98.
DE   RecName: Full=Sucrose-6-phosphate hydrolase;
DE            Short=Sucrase;
DE            EC=3.2.1.26;
DE   AltName: Full=Invertase;
GN   Name=scrB;
OS   Staphylococcus xylosus.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1288;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 20267 / Isolate C2A;
RX   PubMed=8423155; DOI=10.1128/jb.175.3.851-857.1993;
RA   Brueckner R., Wagner E., Goetz F.;
RT   "Characterization of a sucrase gene from Staphylococcus xylosus.";
RL   J. Bacteriol. 175:851-857(1993).
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   ---------------------------------------------------------------------------
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; X67744; CAA47970.1; -; Genomic_DNA.
DR   PIR; A47059; A47059.
DR   RefSeq; WP_047172114.1; NZ_CP171612.1.
DR   AlphaFoldDB; Q05936; -.
DR   SMR; Q05936; -.
DR   STRING; 1288.AWC37_07650; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   PaxDb; 1288-AWC37_07650; -.
DR   KEGG; sxo:SXYL_00887; -.
DR   eggNOG; COG1621; Bacteria.
DR   BioCyc; MetaCyc:MONOMER-12602; -.
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..494
FT                   /note="Sucrose-6-phosphate hydrolase"
FT                   /id="PRO_0000169875"
FT   ACT_SITE        48
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   BINDING         45..48
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         64
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         107..108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         168..169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   494 AA;  57371 MW;  3F129C33DC1DAB78 CRC64;
     MSEWTKEQRY QKYEDVDQQT IEKLTEQVNQ SEYRQTFHIQ PQIGLLNDPN GLIYFKGNYY
     VSHQWFPLGP VHGLKYWYTY QSKDLVDFKA IGPTIKPDTK DDSHGVYSGS AFEYHDHLYY
     MYTANHRDSD WNRISTQHIA KMSKDGSINK FPKAVISAPP SGYTQHFRDP KVHVQDGVYY
     AMIAAQNIKK QGRILQYRST DIVNWEFQGE VQTNLDDFGY MWECPDYFNL NGYDMLLFCP
     QGIDSEGERF KNIYQSGYIM GQYDINNLTM NHADFHELDY GFDFYAPQTF LDENGQRILI
     GWMGLPDINY PSDADGWAHC LTIPRVLTIE SGNLKQRPIK ALEKLRTNEE TALGYANKFT
     RQLHPYEGKQ FELIIDILEN EATEVYFEVR TSKTESTLIT YNKREQKLTL DRSESGQLPE
     PVEGTTRSTY LDTPLSKLQL FVDTSSVEIF CNDGERVMTA RIFTDENATG IKTSTESGQT
     YLKFTKYDLK GDTI
//