SCRB_VIBC3
ID SCRB_VIBC3 Reviewed; 546 AA.
AC A5EZZ8; C3M5S8;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Probable sucrose-6-phosphate hydrolase;
DE Short=Sucrase;
DE EC=3.2.1.26;
DE AltName: Full=Invertase;
GN Name=cscA; OrderedLocusNames=VC0395_0599, VC395_A0657;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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; CP000626; ABQ18842.1; -; Genomic_DNA.
DR EMBL; CP001236; ACP11491.1; -; Genomic_DNA.
DR RefSeq; WP_000923294.1; NZ_JAACZH010000013.1.
DR AlphaFoldDB; A5EZZ8; -.
DR SMR; A5EZZ8; -.
DR STRING; 345073.VC395_A0657; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR EnsemblBacteria; ABQ18842; ABQ18842; VC0395_0599.
DR KEGG; vco:VC0395_0599; -.
DR KEGG; vcr:VC395_A0657; -.
DR PATRIC; fig|345073.21.peg.3393; -.
DR eggNOG; COG1621; Bacteria.
DR HOGENOM; CLU_001528_7_1_6; -.
DR OMA; WMGVPDG; -.
DR UniPathway; UPA00238; -.
DR Proteomes; UP000000249; Chromosome 1.
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_0000341299"
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; 62312 MW; 8F7360DCCEC6B2CC CRC64;
MLLDTLLELA GGINNVTRIL APQGQVVLAL KHPPHAPHLP DDVSLQSVLG EWQLSVQRTA
EVSDQQLAAI GKAIAERQKR ATLPYQTALD CPYRPQWHIS PPQGLLNDPN GFIYHQEEYH
LFYQWHPFAC EHKDKYWVHL KSLDLVHWQW QSVALTPSDW FDSHGVFSGH AVSHQQDLWL
FYTGNTRLGT ERQRQTMQCA ARMNANGEFE KLGPVIRCLP EGVTEHIRDP KVIYTQGKWQ
MLLGAQTLAH QGRLAVYHSD DLLHWHFDKL YGDELGDYGY MWECPDWFEL QGEAFFVFGP
QGIASANPHH TIEHQNRIFR ATQNAQGEIA LLQGWPLDEG FDFYAPQTAQ TADGRRVLCG
WMGLPDETQH PSCDQGWIHQ LTALRELEWR EGKIYQHPLR ELDTLQSEPH TLLLSDTVTE
LKTKSFDLQV TLPWGCELRL MQNAQYCVTL TLDAENRLLR LDRSATQIRQ GDTIRELKLD
SPTVELRILA DQSSLEIFIN QGEHVMTSRI FTPLDATGIS LHGASVDAKL YYMAPASAPF
NLEVNV