ID   SCRB_KLEPN              Reviewed;         466 AA.
AC   P27217;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Sucrose-6-phosphate hydrolase;
DE            Short=Sucrase;
DE            EC=3.2.1.26;
DE   AltName: Full=Invertase;
GN   Name=scrB;
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1033-5P14 / KAY2026;
RX   PubMed=8628219; DOI=10.1007/bf02174179;
RA   Titgemeyer F., Jahreis K., Ebner R., Lengeler J.W.;
RT   "Molecular analysis of the scrA and scrB genes from Klebsiella pneumoniae
RT   and plasmid pUR400, which encode the sucrose transport protein Enzyme II
RT   Scr of the phosphotransferase system and a sucrose-6-phosphate invertase.";
RL   Mol. Gen. Genet. 250:197-206(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-29, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=ATCC 23357 / A-11;
RX   PubMed=11473129; DOI=10.1074/jbc.m106504200;
RA   Thompson J., Robrish S.A., Immel S., Lichtenthaler F.W., Hall B.G.,
RA   Pikis A.;
RT   "Metabolism of sucrose and its five linkage-isomeric alpha-D-glucosyl-D-
RT   fructoses by Klebsiella pneumoniae. Participation and properties of
RT   sucrose-6-phosphate hydrolase and phospho-alpha-glucosidase.";
RL   J. Biol. Chem. 276:37415-37425(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 316-466.
RC   STRAIN=1033-5P14 / KAY2026;
RX   PubMed=8412665; DOI=10.1111/j.1365-2958.1993.tb01681.x;
RA   Jahreis K., Lengeler J.W.;
RT   "Molecular analysis of two ScrR repressors and of a ScrR-FruR hybrid
RT   repressor for sucrose and D-fructose specific regulons from enteric
RT   bacteria.";
RL   Mol. Microbiol. 9:195-209(1993).
CC   -!- FUNCTION: Hydrolyzes sucrose and sucrose-6P, but fails to hydrolyze any
CC       of the phosphorylated isomers of sucrose and other phospho-D-
CC       glucosides, including maltose-6'P and trehalose-6P.
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.
CC   -!- MASS SPECTROMETRY: Mass=52581; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:11473129};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR   EMBL; X57401; CAA40659.1; -; Genomic_DNA.
DR   EMBL; X67751; CAA47976.1; -; Genomic_DNA.
DR   PIR; S62332; S62332.
DR   RefSeq; WP_004191473.1; NZ_WVVY01000005.1.
DR   AlphaFoldDB; P27217; -.
DR   SMR; P27217; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   BioCyc; MetaCyc:MON-12621; -.
DR   BRENDA; 3.2.1.B3; 2814.
DR   SABIO-RK; P27217; -.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cytoplasm; Direct protein sequencing; Glycosidase;
KW   Hydrolase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11473129"
FT   CHAIN           2..466
FT                   /note="Sucrose-6-phosphate hydrolase"
FT                   /id="PRO_0000169872"
FT   ACT_SITE        41
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   BINDING         38..41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         100..101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         159..160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         218
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   466 AA;  52708 MW;  9CE446CE2DB1F075 CRC64;
     MSLPSRLPAI LQAVMQGQPQ ALADSHYPQW HLAPVNGLLN DPNGFCQVAG RYHLFYQWNP
     LACDHTYKCW GHWSSADLLH WRHEPIALMP DEEYDRNGCY SGSAVEFEGA LTLCYTGNVK
     FPDGGRTAWQ CLATENADGT FRKLGPVLPL PEGYTGHVRD PKVWRQDGRW YMVLGAQDVQ
     QRGKVLLFTA SDLREWRLVG EIAGHDVNGL ANAGYMWECP DLFPLADTHL LICCPQGLAR
     EAQRFLNTYP AVWMAGRFDA ERGIFDHGPL HELDSGFEFY APQTMQADDG RRLLVGWMGV
     PDGDEMHQPT RAQGWIHQMT CVRELEWQAG TLYQRPLREL VALRGEAQGW CGQTLPLAPM
     ELAFDLSPDS TLGLDFAGAL QLTVNRDGLR LSRRGLQTAE MHHRYWRGEA RRLRIFIDRS
     SVEIFINDGE GVMSSRFFPG YPGQLIFSGA TPVAFCRWLL RPCMVE