ID   SCRB_STRMU              Reviewed;         479 AA.
AC   P13522;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2002, sequence version 3.
DT   03-AUG-2022, entry version 138.
DE   RecName: Full=Sucrose-6-phosphate hydrolase;
DE            Short=Sucrase;
DE            EC=3.2.1.26;
DE   AltName: Full=Invertase;
GN   Name=scrB; OrderedLocusNames=SMU_1843;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GS-5;
RX   PubMed=3397182; DOI=10.1128/iai.56.8.1956-1960.1988;
RA   Sato Y., Kuramitsu H.K.;
RT   "Sequence analysis of the Streptococcus mutans scrB gene.";
RL   Infect. Immun. 56:1956-1960(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-9.
RC   STRAIN=GS-5;
RX   PubMed=2536656; DOI=10.1128/jb.171.1.263-271.1989;
RA   Sato Y., Poy F., Jacobson G.R., Kuramitsu H.K.;
RT   "Characterization and sequence analysis of the scrA gene encoding enzyme
RT   IIScr of the Streptococcus mutans phosphoenolpyruvate-dependent sucrose
RT   phosphotransferase system.";
RL   J. Bacteriol. 171:263-271(1989).
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 {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR   EMBL; M36849; AAA26972.1; -; Genomic_DNA.
DR   EMBL; X51507; CAA35872.1; -; Genomic_DNA.
DR   EMBL; AE014133; AAN59465.1; -; Genomic_DNA.
DR   EMBL; M22711; AAA26970.2; -; Genomic_DNA.
DR   PIR; A43501; A43501.
DR   RefSeq; NP_722159.1; NC_004350.2.
DR   RefSeq; WP_002262658.1; NC_004350.2.
DR   AlphaFoldDB; P13522; -.
DR   SMR; P13522; -.
DR   STRING; 210007.SMU_1843; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   PRIDE; P13522; -.
DR   EnsemblBacteria; AAN59465; AAN59465; SMU_1843.
DR   KEGG; smu:SMU_1843; -.
DR   PATRIC; fig|210007.7.peg.1645; -.
DR   eggNOG; COG1621; Bacteria.
DR   HOGENOM; CLU_001528_7_1_9; -.
DR   OMA; WMGVPDG; -.
DR   PhylomeDB; P13522; -.
DR   BRENDA; 3.2.1.B3; 5941.
DR   SABIO-RK; P13522; -.
DR   UniPathway; UPA00238; -.
DR   Proteomes; UP000002512; Chromosome.
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;
KW   Reference proteome.
FT   CHAIN           1..479
FT                   /note="Sucrose-6-phosphate hydrolase"
FT                   /id="PRO_0000169876"
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         166..167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        188..212
FT                   /note="Missing (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   479 AA;  54672 MW;  D44A6810CB68CA1C CRC64;
     MNLPQNIRYR RYQDWTEEEI KSIKTNVALS PWHTTYHIEP KTGLLNDPNG FSYFNGKFNL
     FYQNWPFGAA HGLKSWIHTE SEDLVHFKET GTVLYPDTSH DSHGAYSGSA YEIGDQLFLF
     YTGNVRDENW VRHPLQIGAF MDKKGNIQKF TDVLIKQPND VTEHFRDPQI FNYKGQFYAI
     VGAQSLDKKG FIKLYKAVDN DIKNWQEVGN LDFGGSKSEY MIECPNLVFI NEQPVLIYSP
     QGLSKSELDY HNIYPNTYKV CQSFDTEKPA LVDASEIQNL DFGFECYATQ AFNAPDGRVY
     AVSWIGLPDI DYPSDSYDYQ GALSLVKELS LKHGKLYQYP VEAVRSLRSE KEAVTYKPET
     NNTYELELTF DSSSVNELLL FADNKGNGLA ITVDTKMGTI LIDRSKAGEQ YALEFGSQRS
     CSIQAKETVV NIFVDKSIFE IFINKGEKVF TGRVFPNDKQ TGIVIKSGKP SGNYYELKY