ID   SCRB_VIBCH              Reviewed;         548 AA.
AC   Q9KLT6;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Probable sucrose-6-phosphate hydrolase;
DE            Short=Sucrase;
DE            EC=3.2.1.26;
DE   AltName: Full=Invertase;
GN   OrderedLocusNames=VC_A0655;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003853; AAF96556.1; -; Genomic_DNA.
DR   PIR; H82432; H82432.
DR   RefSeq; NP_233044.1; NC_002506.1.
DR   RefSeq; WP_000923309.1; NZ_LT906615.1.
DR   AlphaFoldDB; Q9KLT6; -.
DR   SMR; Q9KLT6; -.
DR   STRING; 243277.VC_A0655; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   DNASU; 2612580; -.
DR   EnsemblBacteria; AAF96556; AAF96556; VC_A0655.
DR   GeneID; 57742050; -.
DR   KEGG; vch:VC_A0655; -.
DR   PATRIC; fig|243277.26.peg.3283; -.
DR   eggNOG; COG1621; Bacteria.
DR   HOGENOM; CLU_001528_7_1_6; -.
DR   OMA; WMGVPDG; -.
DR   BioCyc; VCHO:VCA0655-MON; -.
DR   UniPathway; UPA00238; -.
DR   Proteomes; UP000000584; Chromosome 2.
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; Reference proteome.
FT   CHAIN           1..548
FT                   /note="Probable sucrose-6-phosphate hydrolase"
FT                   /id="PRO_0000341297"
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   548 AA;  62513 MW;  EFA5328C3B66E03D CRC64;
     MLLDTLLELA GGINNVTRIL APQGQVVLAL KHPPLVPHLP DDVSLQSVLG EWQLSVQRTA
     EVSDQQLAAI GKAIAERQKL ETLPYQTALD CPYRPLWHIS PPQGLLNDPN GFIYHQGEYH
     LFYQWHPFAC EHKDKYWVHL KSLDLVDWQW QSVALTPSDW FDSHGVFSGH AVSHQQDLWL
     FYTGNTRLGV DRQRQTMQCA ARMNANGEFE KLGPVIRCLP EGVTEHIRDP KVIYTQGKWQ
     MLLGAQTLAH QGRLAVYHSD DLLHWHFDKL YGDELGDYGY MWECPDWFEL QGEAFFVFGP
     QGIASANPHH TIEHQNRIFR ATQNAQGEIA LLQGWPLDEG FDFYAPQTAQ TADGRRVLCG
     WMGLPDETQH PSCDQGWIHQ LTALRELEWR EGRIYQHPLR ELDTLQSEPH TLLLSDNVTE
     LKTKSFALQV TLPWGCELRL MQNTQYRVTL TLDAENQLLR LDRSATQIRQ GDTIRELKLD
     SPTVELRILA DQSSLEIFIN QGEHVMTSRI FTPRDASGIS LHGASVDAKL YYMAPASAPF
     NLEVNVQP