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SCRB_VIBCL
ID   SCRB_VIBCL              Reviewed;         546 AA.
AC   Q56660;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Probable sucrose-6-phosphate hydrolase;
DE            Short=Sucrase;
DE            EC=3.2.1.26;
DE   AltName: Full=Invertase;
OS   Vibrio cholerae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=BV6;
RA   Chon S.Y.;
RL   Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Enables the bacterium to metabolize sucrose as a sole carbon
CC       source. {ECO:0000250}.
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 {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR   EMBL; M74035; AAA27560.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q56660; -.
DR   SMR; Q56660; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
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   3: Inferred from homology;
KW   Cytoplasm; Glycosidase; Hydrolase.
FT   CHAIN           1..546
FT                   /note="Probable sucrose-6-phosphate hydrolase"
FT                   /id="PRO_0000341298"
FT   ACT_SITE        108
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   BINDING         105..108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         167..168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         228..229
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   546 AA;  62334 MW;  BC6FF116B1A40CB4 CRC64;
     MLLDTQLELA GGINNVTRIL APQGQVVLAL KHPPHAPHLP DDVSLQSVLG EWQLSVQRTA
     EVSDQQLATI GKAISERQKL ETLPYQTALD CPYRPLWHIS PPQGLLNDPN GFIYHQGEYH
     LFYQWHPFVC EHKDKYWVHL KSLDLVHWQW QSVALTPSDW FDSHGVFSGH AVSHQQDLWL
     FYTGNTRLGV DRQRQTMQCA ARMNANGEFE KLGPVIRCLP EGVTEHIRDP KVIYTQGKWH
     MLLGAQTLAH QGRLAVYHSD DLLHWHFDKL YGDELGNYGY MWECPDWFEL QGEAFFVFGP
     QGIASANPHH TIEHQNRIFR ATQNAQGEIA LLQGWPLDEG FDFYAPQTAQ TTDGRRVLCG
     WMGLPDETQH PSCDQGWIHQ LTALRELEWR EGKIYQHPLR ELDTLRSEPH TLLLSDTVTE
     LKAKSFDVQV TLPWGCQLRL MQNAQYCVTL TLDAENRLLR LDRSATQIRQ GDTIRELKLD
     SPTVELRILA DQSSLEIFIN QGEHVMTSRI FTPLDATGIS LHGASVDAKL YYMAPASAPF
     NLEVNV
 
 
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