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Database: UniProt
Entry: A0A1G8STM4_9BACI
LinkDB: A0A1G8STM4_9BACI
Original site: A0A1G8STM4_9BACI 
ID   A0A1G8STM4_9BACI        Unreviewed;       482 AA.
AC   A0A1G8STM4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=SAMN04490247_1518 {ECO:0000313|EMBL:SDJ32513.1};
OS   Salimicrobium halophilum.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Salimicrobium.
OX   NCBI_TaxID=86666 {ECO:0000313|EMBL:SDJ32513.1, ECO:0000313|Proteomes:UP000199225};
RN   [1] {ECO:0000313|EMBL:SDJ32513.1, ECO:0000313|Proteomes:UP000199225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 4771 {ECO:0000313|EMBL:SDJ32513.1,
RC   ECO:0000313|Proteomes:UP000199225};
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; FNEV01000004; SDJ32513.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8STM4; -.
DR   STRING; 86666.SAMN04490247_1518; -.
DR   UniPathway; UPA00238; -.
DR   Proteomes; UP000199225; 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; 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}.
FT   DOMAIN          31..329
FT                   /note="Glycosyl hydrolase family 32 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00251"
FT   DOMAIN          344..470
FT                   /note="Glycosyl hydrolase family 32 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08244"
SQ   SEQUENCE   482 AA;  56150 MW;  BF0E41329A50F419 CRC64;
     MEEQELRKAI RDEVHKQKET VENDPHRQAY HLMAPVGLIN DPNGLIKWGE DYHLFFQWSP
     FQPGHGTKVW GHYHTKDFVN YTLEEPALVP TEWYDKDGCF SGSAVEEDGK LYLFYTGNTE
     ENGDILEEYQ TAAVSEDGNS FRKQGVLIEK PEGITPHFRD PKVWKEGDTW YMVVGAQTED
     RRGAVLLYTS EDLQQWTYMK RLAEAGDEEG YMWECPDFFR LDGLDILLFS PQGIEPDDIH
     FHNVYQSGYV IGRTKGDRWE RGDFHELDHG FEFYAPQTFE ADGRRIMIGW MGVPDQYEEA
     HPTVANQWIH SWTIPRELTW NGERIVQTPI METKAWRTSE IPVERTETIE NDQREVEDVG
     GRVMEVAIDF EEIGDMWAIE LYHEASLSYK KSRNLLTLSR PHPEDAEKTQ FRHVQLDKPL
     KSLRMFFDYS SFEVFVNEGE EVFTSRIFAD AALTDLAFTS LGTSTFHVKK WELAPIEIDS
     KL
//
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