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Database: UniProt
Entry: A0A1G6CXL8_9STRE
LinkDB: A0A1G6CXL8_9STRE
Original site: A0A1G6CXL8_9STRE 
ID   A0A1G6CXL8_9STRE        Unreviewed;       479 AA.
AC   A0A1G6CXL8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
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=SAMN02910293_01848 {ECO:0000313|EMBL:SDB37550.1};
OS   Streptococcus henryi.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=439219 {ECO:0000313|EMBL:SDB37550.1, ECO:0000313|Proteomes:UP000182508};
RN   [1] {ECO:0000313|EMBL:SDB37550.1, ECO:0000313|Proteomes:UP000182508}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A-4 {ECO:0000313|EMBL:SDB37550.1,
RC   ECO:0000313|Proteomes:UP000182508};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FMXP01000028; SDB37550.1; -; Genomic_DNA.
DR   RefSeq; WP_074486451.1; NZ_FMXP01000028.1.
DR   AlphaFoldDB; A0A1G6CXL8; -.
DR   STRING; 439219.SAMN02910293_01848; -.
DR   eggNOG; COG1621; Bacteria.
DR   UniPathway; UPA00238; -.
DR   Proteomes; UP000182508; Unassembled WGS sequence.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182508}.
FT   DOMAIN          37..340
FT                   /note="Glycosyl hydrolase family 32 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00251"
FT   DOMAIN          348..473
FT                   /note="Glycosyl hydrolase family 32 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08244"
SQ   SEQUENCE   479 AA;  54588 MW;  0D66346DDBD1B53A CRC64;
     MDMPQNVRYR AYSDWTSQEI QEINNNVKKS PWHATYHIEP KTGLLNDPNG FSFFNGKYTL
     FYQNWPFGAA HGLKQWVHTE SEDLVHFTET AVRLLPDHAH DSHGAYSGSA YEIDGKLFLF
     YTGNVRDENW VRDPLQIGAW MDKEGKIEKF ENVLIQQPND VTEHFRDPQI FEYKGQFFAI
     VGAQSLDKKG FIKLYKAVEN NVENWEFVGD LKFGGTGSEY MIECPNLVFV DDKPVLLYSP
     QGLDKSELDY DNIYPNTYKI CQTFDTKNAE LIGASEILNL DYGFEAYATQ GFNAPDGRTL
     IVSWIGLPDV DYPTDKYDYQ GAMSLVKELT IKDGKLYQYP VETITSLRDS EENFSEKSTT
     SNTYELEVTF PANDKSELLL FADDKGNGLR LTVDTKEGIV TLDRSKAGVQ YATDFGTSRH
     CSIDKDETTA NIFVDKSIVE IFINKGEKVF TSRVFPEEGQ NGIQIVSGKP SGKYFELKY
//
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