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Database: UniProt
Entry: A0A1I4AVV8_HALDA
LinkDB: A0A1I4AVV8_HALDA
Original site: A0A1I4AVV8_HALDA 
ID   A0A1I4AVV8_HALDA        Unreviewed;       485 AA.
AC   A0A1I4AVV8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=SAMN04487936_12120 {ECO:0000313|EMBL:SFK60011.1};
OS   Halobacillus dabanensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX   NCBI_TaxID=240302 {ECO:0000313|EMBL:SFK60011.1, ECO:0000313|Proteomes:UP000183557};
RN   [1] {ECO:0000313|EMBL:SFK60011.1, ECO:0000313|Proteomes:UP000183557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.3704 {ECO:0000313|EMBL:SFK60011.1,
RC   ECO:0000313|Proteomes:UP000183557};
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; FOSB01000021; SFK60011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4AVV8; -.
DR   UniPathway; UPA00238; -.
DR   Proteomes; UP000183557; 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}.
FT   DOMAIN          33..338
FT                   /note="Glycosyl hydrolase family 32 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00251"
FT   DOMAIN          345..476
FT                   /note="Glycosyl hydrolase family 32 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08244"
SQ   SEQUENCE   485 AA;  56042 MW;  B41352F450E346B6 CRC64;
     MSERDLELKS LAEQEIEKHK ETVATDPYRL NYHHMPPVGL MNDPNGLIQW RGVYHLFYQW
     MPFDTTHGAK FWGHYTSENL VNWKHEKIAL APSDTFDRDG VYSGSAISHE GRLYLFYTGN
     LDGKNGPEQE NQCLAVSEDG VTFEKKGVLI ETPEGYTAHF RDPKVWKQGD IWYMVVGAQS
     EDHQGKAVMF SSHDLHNWEH LGTIAGSKEG RNGELGFMWE CPDIFELGGK DILMVCPQGL
     ESDGMNYANT YQSGYFAGEM NEHNLQFNHS EFRELDRGFE FYAPQTTVDE KGRRILFGWM
     GVPEQYEQEH PTIEKHWVHC MTIPRELTWN GEKITQTPVE ELSAMRGPVL LHSSVTIEND
     QKAIRGIQGR SIELNIEIDQ LNEMFAIELF QYASLSYKDR ILTLSRPHLE ERSKTEFRRV
     GLGEGLRNIR LFIDRSSLEV FVNDGEEVFT SRIFPQPEEE HILFTSLGST TFSIEKWDLN
     GYQYE
//
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