ID R9LQ71_9FIRM Unreviewed; 478 AA.
AC R9LQ71;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=C815_01172 {ECO:0000313|EMBL:EOS60713.1};
OS Firmicutes bacterium M10-2.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1235796 {ECO:0000313|EMBL:EOS60713.1, ECO:0000313|Proteomes:UP000014154};
RN [1] {ECO:0000313|EMBL:EOS60713.1, ECO:0000313|Proteomes:UP000014154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M10-2 {ECO:0000313|EMBL:EOS60713.1,
RC ECO:0000313|Proteomes:UP000014154};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Firmicutes bacterium M10-2.";
RL Submitted (APR-2013) 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}.
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:EOS60713.1}.
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DR EMBL; ASTB01000025; EOS60713.1; -; Genomic_DNA.
DR AlphaFoldDB; R9LQ71; -.
DR STRING; 1235796.C815_01172; -.
DR PATRIC; fig|1235796.3.peg.1171; -.
DR eggNOG; COG1621; Bacteria.
DR HOGENOM; CLU_001528_7_1_9; -.
DR UniPathway; UPA00238; -.
DR Proteomes; UP000014154; 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:UP000014154}.
FT DOMAIN 31..341
FT /note="Glycosyl hydrolase family 32 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00251"
FT DOMAIN 420..469
FT /note="Glycosyl hydrolase family 32 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08244"
SQ SEQUENCE 478 AA; 56248 MW; 13C82912FB34E79C CRC64;
MMTKEMYKKK MEKECEQKRI VESDPYRLKF HIQPPMGWLN DPNGLFEKDG IFHIYYQYSP
FEPQGGTKLW GHYTTEDFIE FKEHEPFLFA DWRYDERGVY SGSAFVEDGT IHYFYTGNVK
LFDRDDYDYC NNGREQNTIH ITSLDGFSHS EKQLIMTDRD YPADMSCHVR DPKIFKKSGI
YYMVLGGRDV NSHGCLLIYR SEDLENWEEF DRLSIPDFGY MWECPDLFEL DGELFLVFSP
QGLEEDGLNN RNIYQTGYCK LDYDFQTKQC TFSKFQELDR GFDYYAPQSF EDEQGRRIQF
GWMGMGDATY TNEPTIEKGW QHAFTLPRQL HAENGHIYQM PIEELKNLRD KTYRSTIGDF
KDPNFGPCIE WDIQFDESVP FTIKMYGDIE ISYDGKLLKM SMAESGYGRD WRAIEIDQIK
DLKIMLDTSS IEMFVNNGWT VFSSRMYPKT AMNLSIESAS EGTVAIHSLD SVKIENNE
//
