ID   SCRB_SALTM              Reviewed;         466 AA.
AC   P37075;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Sucrose-6-phosphate hydrolase;
DE            Short=Sucrase;
DE            EC=3.2.1.26;
DE   AltName: Full=Invertase;
GN   Name=scrB;
OS   Salmonella typhimurium.
OG   Plasmid pUR400.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8412665; DOI=10.1111/j.1365-2958.1993.tb01681.x;
RA   Jahreis K., Lengeler J.W.;
RT   "Molecular analysis of two ScrR repressors and of a ScrR-FruR hybrid
RT   repressor for sucrose and D-fructose specific regulons from enteric
RT   bacteria.";
RL   Mol. Microbiol. 9:195-209(1993).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=8628219; DOI=10.1007/bf02174179;
RA   Titgemeyer F., Jahreis K., Ebner R., Lengeler J.W.;
RT   "Molecular analysis of the scrA and scrB genes from Klebsiella pneumoniae
RT   and plasmid pUR400, which encode the sucrose transport protein Enzyme II
RT   Scr of the phosphotransferase system and a sucrose-6-phosphate invertase.";
RL   Mol. Gen. Genet. 250:197-206(1996).
CC   -!- FUNCTION: Enables the bacterium to metabolize sucrose as a sole carbon
CC       source.
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   -!- SUBCELLULAR LOCATION: Cytoplasm.
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; X67750; CAA47974.1; -; Genomic_DNA.
DR   PIR; S62330; S62330.
DR   AlphaFoldDB; P37075; -.
DR   SMR; P37075; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   UniPathway; UPA00238; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004564; F:beta-fructofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005985; P:sucrose metabolic process; IEA:UniProtKB-UniPathway.
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   InterPro; IPR006232; Suc6P_hydrolase.
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   TIGRFAMs; TIGR01322; scrB_fam; 1.
DR   PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase; Plasmid.
FT   CHAIN           1..466
FT                   /note="Sucrose-6-phosphate hydrolase"
FT                   /id="PRO_0000169877"
FT   ACT_SITE        41
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   BINDING         38..41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         100..101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         159..160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   466 AA;  52589 MW;  A62CB3F53726138B CRC64;
     MSLPSRLPAI LQAVMQGQPR ALADSHYPRW HHAPVTGLMN DPNGFIEFAG RYHLFYQWNP
     LACDHTFKCW AHWSSIDLLH WQHEPIALMP DEEYDRNGCY SGSAVDNNGT LTLCYTGNVK
     FAEGGRTAWQ CLATENADGT FRKIGPVLPL PEGYTGHVRD PKVWRHEDLW YMVLGAQDRQ
     KRGKVLLFSS ADLHQWTSMG EIAGHGINGL DDVGYMWECP DLFPLGDQHI LICCPQGIAR
     EEECYLNTYP AVWMAGEFDY AAGAFRHGEL HELDAGFEFY APQTMLTSDG RRLLVGWMGV
     PEGEEMLQPT LNNGWIHQMT CLRELEFING QLYQRPLREL SALRGEANGW SGNALPLAPM
     EIDLQTRGGD MLSLDFGGVL TLECDASGLR LARRSLASDE MHYRYWRGNV RSLRVFIDQS
     SVEIFINGGE GVMSSRYFPA CSGQLTFSGI TPDAFCYWPL RTCMVE