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Database: UniProt
Entry: T0TZI0_9STRE
LinkDB: T0TZI0_9STRE
Original site: T0TZI0_9STRE 
ID   T0TZI0_9STRE            Unreviewed;       484 AA.
AC   T0TZI0;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 39.
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   ORFNames=HSISM1_1990 {ECO:0000313|EMBL:EQC76371.1};
OS   Streptococcus sp. HSISM1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1316408 {ECO:0000313|EMBL:EQC76371.1};
RN   [1] {ECO:0000313|EMBL:EQC76371.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HSISM1 {ECO:0000313|EMBL:EQC76371.1};
RA   Van den Bogert B., Boekhorst J., Herrmann R., Smid E.J., Zoetendal E.G.,
RA   Kleerebezem M.;
RT   "Comparative Genomics Analysis of Streptococcus Isolates from the Human
RT   Small Intestine Reveals their Adaptation to a Highly Dynamic Ecosystem.";
RL   PLoS ONE 8:E83418-E83418(2013).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EQC76371.1}.
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DR   EMBL; ASKI01000069; EQC76371.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0TZI0; -.
DR   PATRIC; fig|1316408.3.peg.1541; -.
DR   eggNOG; COG1621; Bacteria.
DR   HOGENOM; CLU_001528_7_1_9; -.
DR   UniPathway; UPA00238; -.
DR   Proteomes; UP000015933; 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   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   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 {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}.
FT   DOMAIN          37..340
FT                   /note="Glycosyl hydrolase family 32 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00251"
FT   DOMAIN          355..468
FT                   /note="Glycosyl hydrolase family 32 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08244"
SQ   SEQUENCE   484 AA;  54995 MW;  41C20746E733DD3E CRC64;
     MEWTTERRYR RYEDWTTEEK QAIQENMAKS PWHTHYHVEP KAGLLNDPNG FSYFDGKWIL
     FYQNFPFGAA HGLKSWVQTE SEDLVHFTET GVTLLPDTDL DSHGAYSGSA MQFGDKLFLF
     YTGNVRDAEW VRHPYQVGAL MDKDGKIEKI DKILIDQPAD STDHFRDPQI FNFKGQYYAI
     VGGQDLEKKG FIRLYKAVDN DYTNWVAVGD LDFANDRTAY MMECPNLVFV GDQPVLLYCP
     QGLDKSVLDY DNIYPNMYKI GASFDPENAK MVDVSELHNL DYGFEAYATQ GFNAPDGRAY
     AVSWLGLPDV SYPTDSYDYQ GALSLVKELT IKDGKLYQYP VEAIKDLRAE SEEFANKAQT
     KNCYELELQF EKDSQNEIVL FADAEGKGLA LTFDLAKGLV TVDRSQAGEQ YAQEFGTSRS
     CPIANQTTTA NIFIDNSIFE IFINKGEKVF SGRVYPHADQ NGILIKSGTP TGTYYELDYG
     RKAN
//
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