ID   CSCA_ECOLX              Reviewed;         477 AA.
AC   P40714;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=Sucrose-6-phosphate hydrolase;
DE            Short=Sucrase;
DE            EC=3.2.1.26;
DE   AltName: Full=Invertase;
GN   Name=cscA;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=EC3132;
RX   PubMed=12218016; DOI=10.1128/jb.184.19.5307-5316.2002;
RA   Jahreis K., Bentler L., Bockmann J., Hans S., Meyer A., Siepelmeyer J.,
RA   Lengeler J.W.;
RT   "Adaptation of sucrose metabolism in the Escherichia coli wild-type strain
RT   EC3132.";
RL   J. Bacteriol. 184:5307-5316(2002).
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}.
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DR   EMBL; X81461; CAA57219.1; -; Genomic_DNA.
DR   PIR; S52162; S52162.
DR   AlphaFoldDB; P40714; -.
DR   SMR; P40714; -.
DR   STRING; 585034.ECIAI1_2428; -.
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.
FT   CHAIN           1..477
FT                   /note="Sucrose-6-phosphate hydrolase"
FT                   /id="PRO_0000169879"
FT   ACT_SITE        39
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   BINDING         36..39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         55
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         98..99
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         160..161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         298
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   477 AA;  54363 MW;  48E6622AEA380EBD CRC64;
     MTQSRLHAAQ NALAKLHERR GNTFYPHFHL APPAGWMNDP NGLIWFNDRY HAFYQHHPMS
     EHWGPMHWGH ATSDDMIHWQ HEPIALAPGD ENDKDGCFSG SAVDDNGVLS LIYTGHVWLD
     GAGNDDAIRE VQCLATSRDG IHFEKQGVIL TPPEGIMHFR DPKVWREADT WWMVVGAKDP
     GNTGQILLYR GSSLREWTFD RVLAHADAGE SYMWECPDFF SLGDQHYLMF SPQGMNAEGY
     SYRNRFQSGV IPGMWSPGRL FAQSGHFTEL DNGHDFYAPQ SFVAKDGRRI VIGWMDMWES
     PMPSKREGWA GCMTLARELS ESNGKLLQRP VHEAESLRQQ HQSISPRTIS NKYVLQENAQ
     AVEIQLQWAL KNSDAEHYGL QLGAGMRLYI DNQSERLVLW RYYPHENLDG YRSIPLPQGD
     MLALRIFIDT SSVEVFINDG EAVMSSRIYP QPEERELSLY ASHGVAVLQH GALWQLG