ID   SCRB_VIBAL              Reviewed;         484 AA.
AC   P13394;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Sucrose-6-phosphate hydrolase;
DE            Short=Sucrase;
DE            EC=3.2.1.26;
DE   AltName: Full=Invertase;
GN   Name=scrB;
OS   Vibrio alginolyticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2551785; DOI=10.1016/0378-1119(89)90249-7;
RA   Scholle R.R.;
RT   "Nucleotide sequence and analysis of the Vibrio alginolyticus sucrase gene
RT   (scrB).";
RL   Gene 80:49-56(1989).
CC   -!- FUNCTION: Enables the bacterium to metabolize sucrose as a sole carbon
CC       source.
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:0000255|PROSITE-ProRule:PRU10067};
CC   -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: By sucrose.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR   EMBL; M26511; AAA27562.1; -; Genomic_DNA.
DR   PIR; JU0091; JU0091.
DR   AlphaFoldDB; P13394; -.
DR   SMR; P13394; -.
DR   STRING; 663.BAU10_17445; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   eggNOG; COG1621; Bacteria.
DR   UniPathway; UPA00238; -.
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   Gene3D; 2.115.10.20; -; 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   Pfam; PF08244; Glyco_hydro_32C; 1.
DR   Pfam; PF00251; Glyco_hydro_32N; 1.
DR   SMART; SM00640; Glyco_32; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF75005; SSF75005; 1.
DR   TIGRFAMs; TIGR01322; scrB_fam; 1.
DR   PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase.
FT   CHAIN           1..484
FT                   /note="Sucrose-6-phosphate hydrolase"
FT                   /id="PRO_0000169878"
FT   ACT_SITE        51
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   BINDING         48..51
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         110..111
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         168..169
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         223
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   484 AA;  55657 MW;  A521D006C2118BF4 CRC64;
     MSLNNRWTVE QRYRRLEQIP QCDIEEMTLS RQQDKGFPSF HIAPKFGLLN DPNGLCYFNG
     EHHIFYQWTP VGPVHGMKYW YHLSTKDFIH FTDHGVGLHP DQDYDSHGVY SGGALVENNQ
     VLLFFTGNKR DQNWNRIPTQ CFATMDSDGS IEKHGVVIEN EHYTEHFRDP KVWKKGDDYL
     MVVGAQTKTE HGSMALYQSK DLKTWQHKGP IKTKFSDLGY MWECPDFFEI NGQSVMLFSP
     QGVSSSNPYD FKNIYSVAYI VGDQLNLESM TLENHQDILQ PDYGFDFYAP QTYLDESGRR
     ILIAWIGLPE IDTPSVTHQW AGMLSLPREL TLKDGFLVQT PLPELKSLRK EEVVFAQSHT
     LESTSCLIQL DLVGDGFELE LSNLKGDNIV FSATEHEFML DRRYMSHLYA EEFGGIRKAP
     RLDAKQTIDI YIDNSVIEIF INGGKHTMTS RFFIDDLNKV TLKGLEQARL FPLKGITGLF
     ESAK