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