ID   C0MEC4_STRS7            Unreviewed;       479 AA.
AC   C0MEC4;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   10-JUN-2026, entry version 90.
DE   RecName: Full=Sucrose-6-phosphate hydrolase {ECO:0000256|ARBA:ARBA00019623, ECO:0000256|RuleBase:RU362110};
DE            EC=3.2.1.26 {ECO:0000256|ARBA:ARBA00012758, ECO:0000256|RuleBase:RU362110};
DE   AltName: Full=Invertase {ECO:0000256|ARBA:ARBA00033367, ECO:0000256|RuleBase:RU365015};
GN   OrderedLocusNames=SZO_16160 {ECO:0000313|EMBL:CAX00353.1};
OS   Streptococcus equi subsp. zooepidemicus (strain H70).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553483 {ECO:0000313|EMBL:CAX00353.1, ECO:0000313|Proteomes:UP000001368};
RN   [1] {ECO:0000313|EMBL:CAX00353.1, ECO:0000313|Proteomes:UP000001368}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=H70 {ECO:0000313|EMBL:CAX00353.1,
RC   ECO:0000313|Proteomes:UP000001368};
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA   Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA   Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA   Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA   Maskell D.J., Parkhill J., Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
CC   -!- FUNCTION: Enables the bacterium to metabolize sucrose as a sole carbon
CC       source. {ECO:0000256|RuleBase:RU365015}.
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:0000256|RuleBase:RU362110};
CC   -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC       {ECO:0000256|ARBA:ARBA00004914, ECO:0000256|RuleBase:RU365015}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU365015}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family.
CC       {ECO:0000256|ARBA:ARBA00009902, ECO:0000256|RuleBase:RU362110}.
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DR   EMBL; FM204884; CAX00353.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0MEC4; -.
DR   KEGG; seq:SZO_16160; -.
DR   PATRIC; fig|40041.11.peg.1733; -.
DR   eggNOG; COG1621; Bacteria.
DR   HOGENOM; CLU_001528_7_1_9; -.
DR   UniPathway; UPA00238; -.
DR   Proteomes; UP000001368; 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   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; 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.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU365015};
KW   Cytoplasm {ECO:0000256|RuleBase:RU365015};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU362110};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362110};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001368}.
FT   DOMAIN          37..340
FT                   /note="Glycosyl hydrolase family 32 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00251"
FT   DOMAIN          352..467
FT                   /note="Glycosyl hydrolase family 32 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08244"
SQ   SEQUENCE   479 AA;  54588 MW;  7D075D4BE4D6354B CRC64;
     MDLPRSIRYR PYQEWSKEAY QAIQQKVAQS LWRSHFHIEA RTGLLNDPNG FSYFAGSFQL
     FYQNWPFGAA HGLKQWVHTT STDLVHFTET KTRLLPDHQN DSHGAYSGSA YPIGDKLFLC
     YTGNVRSKDW VRHPLQIGAW MDQSGHITKY EQVLIDKPDD VTEHFRDPQL FTYQDQLYAI
     IGAQNLQQQG IIKLYKANNN DVTSWQFVAD LDFDDSGTAY MIECPNLVFI EDKPVLIFCP
     QGLAKSELDY QNIYPNTYKV FQTFDPKRGK LLGGGPIQNL DFGFEAYATQ AFNSPDGRVL
     AVSWIGLPDI NYPTDKYAYQ GALSLVKELR LKNGRLYQAP VPALSKLRDK SQPFQNKKSS
     SNCYELALTI EAQQTAELLL FADTQQKGLK LTIDTRKGQL TIDRSKAGAQ YAQEFGARRS
     CQIPVNRATL NIYVDKSILE IFVNQGEAVL TSRVFPNEGQ SGIELLKGQV SGYYYEMRY
//