ID   SCRB_PSYIN              Reviewed;         545 AA.
AC   A1STJ9;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Probable sucrose-6-phosphate hydrolase;
DE            Short=Sucrase;
DE            EC=3.2.1.26;
DE   AltName: Full=Invertase;
GN   OrderedLocusNames=Ping_0974;
OS   Psychromonas ingrahamii (strain 37).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Psychromonadaceae; Psychromonas.
OX   NCBI_TaxID=357804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=37;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Staley J.,
RA   Richardson P.;
RT   "Complete sequence of Psychromonas ingrahamii 37.";
RL   Submitted (JAN-2007) 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; CP000510; ABM02814.1; -; Genomic_DNA.
DR   RefSeq; WP_011769377.1; NC_008709.1.
DR   AlphaFoldDB; A1STJ9; -.
DR   SMR; A1STJ9; -.
DR   STRING; 357804.Ping_0974; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   EnsemblBacteria; ABM02814; ABM02814; Ping_0974.
DR   KEGG; pin:Ping_0974; -.
DR   eggNOG; COG1621; Bacteria.
DR   HOGENOM; CLU_001528_7_1_6; -.
DR   OMA; WMGVPDG; -.
DR   OrthoDB; 1622507at2; -.
DR   UniPathway; UPA00238; -.
DR   Proteomes; UP000000639; 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   Cytoplasm; Glycosidase; Hydrolase; Reference proteome.
FT   CHAIN           1..545
FT                   /note="Probable sucrose-6-phosphate hydrolase"
FT                   /id="PRO_0000341296"
FT   ACT_SITE        110
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   BINDING         107..110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         169..170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         230..231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   545 AA;  62259 MW;  5F715B4BA992FECB CRC64;
     MSLFSIIKDC GGIHNIQRVL IPDSRIIIEI HEFELLSAEA KQQAYNLTLK QVTYQQTVIE
     NKDEFGAQLL EIGQLISDQQ RQDITPYTAP VECEFRPDWH ISPPQGLLND PNGFIYHQGQ
     YHLFYQWYPY TCVHKDKYWA HLTSKDLVNW QWQPVALTPS DWFDSYGVFS GHAISQDDLL
     MLFYTGNVRI GEQRDRHTTQ CLATSTDGIH FTKQGPVVPE LPPGVTPHCR DPKVIRHNDR
     WLMLLGVQRE DEIGRLAIYH SEDLKTWTFI ALCGDELGDF GYMWECPDFF TLNQQDFIVI
     GPQGIRSPDK SHTAPHHNGI VKAQLETSGK ALLSDFQPLD YGFDFYAPQS LETPDGRRIM
     CAWMGLPDEI DHPSADNGWV HQLTTMRELS YDNGALIQKP IKELATLRHT PIVLSKDETS
     FDLHSKAFEL QVSMQWGSVL RLHQSESGYC EIRLDSASRR LYIDRSNTLI REGDTVREMS
     LAESDSVQLH IFSDTSSLEV FINEGEAVMS ARVFTDKNST QLSFDGDVQI QACWLLNKAS
     APFIS