ID   SCRB_LACLL              Reviewed;         473 AA.
AC   Q04937;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Sucrose-6-phosphate hydrolase;
DE            Short=Sucrase;
DE            EC=3.2.1.26;
DE   AltName: Full=Invertase;
GN   Name=scrB; Synonyms=sacA;
OS   Lactococcus lactis subsp. lactis (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NIZO R5;
RX   PubMed=1330831; DOI=10.1016/0378-1119(92)90161-h;
RA   Rauch P.J., de Vos W.M.;
RT   "Transcriptional regulation of the Tn5276-located Lactococcus lactis
RT   sucrose operon and characterization of the sacA gene encoding sucrose-6-
RT   phosphate hydrolase.";
RL   Gene 121:55-61(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-12, AND CHARACTERIZATION.
RC   STRAIN=K1;
RX   PubMed=1650362; DOI=10.1016/s0021-9258(18)98724-7;
RA   Thompson J., Nguyen N.Y., Sackett D.L., Donkersloot J.A.;
RT   "Transposon-encoded sucrose metabolism in Lactococcus lactis. Purification
RT   of sucrose-6-phosphate hydrolase and genetic linkage to N5-(L-1-
RT   carboxyethyl)-L-ornithine synthase in strain K1.";
RL   J. Biol. Chem. 266:14573-14579(1991).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.5-7.0.;
CC   -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR   EMBL; M96669; AAA25218.1; -; Genomic_DNA.
DR   PIR; JH0754; JH0754.
DR   AlphaFoldDB; Q04937; -.
DR   SMR; Q04937; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   SABIO-RK; Q04937; -.
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   CHAIN           1..473
FT                   /note="Sucrose-6-phosphate hydrolase"
FT                   /id="PRO_0000169873"
FT   ACT_SITE        47
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   BINDING         44..47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         106..107
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         167..168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         224
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        4
FT                   /note="S -> Q (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   473 AA;  54785 MW;  D055ADF8321072E5 CRC64;
     MKWSTKQRYR TYDSYSESDL ESLRKLALKS PWKSNFHIEP ETGLLNDPNG FSYFNEKWHL
     FYQHFPFGPV HGLKSWVHLV SDDLVHFEKT GLVLYPDTKY DNAGVYSGSA LAFENFLFLI
     YTGNHRGEDW VRTPYQLGAK IDKNNQLVKF TEPLIYPDFS QTTDHFRDPQ IFSFQGQIYC
     LIGAQSSQKN GIIKLYKAIE NNLTDWKDLG NLDFSKEKMG YMIECPNLIF INGRSVLVFC
     PQGLDKSIVK YDNIYPNVYV IADDFTTGSK NQLKNAGQLI NLDEGFDCYA TQSFNAPDGS
     AYAISWLGLP ETSYPTDKYN VQGVLSMVKK LSIKDNKLYQ YPVEKMKELR QMEQDLLLAD
     NNIITSNSYE LEVDFRQQTS TLLSLMTNEK GDSALKVEID KENNTITLIR NYEKRLAHVK
     IEKMNVFIDQ SIFEIFINDG EKVLSDCRVF PNKNQYSIRS QNPIKIKLWE LKK