ID   SCR_ZYMMA               Reviewed;         512 AA.
AC   F8DVG5; P22632; P35636; Q5NNZ4; Q84CM3;
DT   14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Sucrose-6-phosphate hydrolase;
DE            Short=Sucrase;
DE            EC=3.2.1.26;
DE   AltName: Full=Invertase;
GN   Name=sacA; Synonyms=invA; OrderedLocusNames=Zmob_0361;
OS   Zymomonas mobilis subsp. mobilis (strain ATCC 10988 / DSM 424 / LMG 404 /
OS   NCIMB 8938 / NRRL B-806 / ZM1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Zymomonadaceae; Zymomonas.
OX   NCBI_TaxID=555217;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10988 / DSM 424 / CCUG 17860 / LMG 404 / NCIMB 8938 / NRRL
RC   B-806 / ZM1;
RX   PubMed=2254250; DOI=10.1128/jb.172.12.6727-6735.1990;
RA   Gunasekaran P., Karunakaran T., Cami B., Mukundan A.G., Preziosi L.,
RA   Baratti J.;
RT   "Cloning and sequencing of the sacA gene: characterization of a sucrase
RT   from Zymomonas mobilis.";
RL   J. Bacteriol. 172:6727-6735(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10988 / DSM 424 / CCUG 17860 / LMG 404 / NCIMB 8938 / NRRL
RC   B-806 / ZM1;
RX   PubMed=21725006; DOI=10.1128/jb.05395-11;
RA   Pappas K.M., Kouvelis V.N., Saunders E., Brettin T.S., Bruce D., Detter C.,
RA   Balakireva M., Han C.S., Savvakis G., Kyrpides N.C., Typas M.A.;
RT   "Genome sequence of the ethanol-producing Zymomonas mobilis subsp. mobilis
RT   lectotype strain ATCC 10988.";
RL   J. Bacteriol. 193:5051-5052(2011).
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; M62718; AAA27701.1; -; Genomic_DNA.
DR   EMBL; CP002850; AEH62209.1; -; Genomic_DNA.
DR   PIR; A37803; A37803.
DR   RefSeq; WP_014500464.1; NC_017262.1.
DR   AlphaFoldDB; F8DVG5; -.
DR   SMR; F8DVG5; -.
DR   STRING; 555217.Zmob_0361; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   EnsemblBacteria; AEH62209; AEH62209; Zmob_0361.
DR   KEGG; zmm:Zmob_0361; -.
DR   eggNOG; COG1621; Bacteria.
DR   HOGENOM; CLU_001528_7_0_5; -.
DR   OMA; YKAGSGH; -.
DR   UniPathway; UPA00238; -.
DR   Proteomes; UP000001494; Chromosome.
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   Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase.
FT   CHAIN           1..512
FT                   /note="Sucrose-6-phosphate hydrolase"
FT                   /id="PRO_0000414237"
FT   ACT_SITE        43
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   BINDING         40..43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         59
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         102..103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         165..166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         229
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        39
FT                   /note="G -> S (in Ref. 1; AAA27701)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        295..297
FT                   /note="FEA -> LKL (in Ref. 1; AAA27701)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        303..308
FT                   /note="ILIAWF -> NINCMV (in Ref. 1; AAA27701)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        312..314
FT                   /note="ENQ -> KS (in Ref. 1; AAA27701)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   512 AA;  58586 MW;  E36934E9797C6DC9 CRC64;
     MESPSYKNLI KAEDAQKKAG KRLLSSEWYP GFHVTPLTGW MNDPNGLIFF KGEYHLFYQY
     YPFAPVWGPM HWGHAKSRDL VHWETLPVAL APGDSFDRDG CFSGCAVDNN GVLTLIYTGH
     IVLSNDSPDA IREVQCMATS IDGIHFQKEG IVLEKAPMPQ VAHFRDPRVW KENDHWFMVV
     GYRTDDKKHQ GIGHVALYRS ENLKDWIFVK TLLGDNSQLP LGKRAFMWEC PDFFSLGNRS
     VLMFSPQGLK ASGYKNRNLF QNGYILGKWQ APQFTPETSF QELDYGHDFY AAQRFEAKDG
     RQILIAWFDM WENQKPSQRD GWAGCMTLPR KLDLIDNKIV MTPVREMEIL RQSEKIESVV
     TLSDAEHPFT MDSPLQEIEL IFDLEKSNAY QAGLALRCNG KGQETLLYID RSQNRIILDR
     NRSGQNVKGI RSCPLPNTSK VRLHIFLDRS SIEIFVGDDQ TQGLYSISSR IFPDKDSLKG
     RLFAIEGYAV FDSFKRWTLQ DANLAAFSSD AC