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RAFD_ECOLX
ID   RAFD_ECOLX              Reviewed;         476 AA.
AC   P16553;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Raffinose invertase;
DE            Short=Invertase;
DE            EC=3.2.1.26;
GN   Name=rafD;
OS   Escherichia coli.
OG   Plasmid pRSD2.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2556373; DOI=10.1128/jb.171.12.6753-6763.1989;
RA   Aslanidis C., Schmid K., Schmitt R.;
RT   "Nucleotide sequences and operon structure of plasmid-borne genes mediating
RT   uptake and utilization of raffinose in Escherichia coli.";
RL   J. Bacteriol. 171:6753-6763(1989).
CC   -!- FUNCTION: May prevent the potential hasard of excessive sucrose
CC       accumulation.
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   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR   EMBL; M27273; AAA24499.1; -; Genomic_DNA.
DR   PIR; C43717; C43717.
DR   RefSeq; WP_000813695.1; NZ_JABXEI010000134.1.
DR   AlphaFoldDB; P16553; -.
DR   SMR; P16553; -.
DR   CAZy; GH32; Glycoside Hydrolase Family 32.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004564; F:beta-fructofuranosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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   Glycosidase; Hydrolase; Plasmid.
FT   CHAIN           1..476
FT                   /note="Raffinose invertase"
FT                   /id="PRO_0000169869"
FT   ACT_SITE        38
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10067"
FT   BINDING         35..38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         97..98
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         159..160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         297
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   476 AA;  54327 MW;  59DF112E9A63723C CRC64;
     MKQRLSLAQS ALEKLSARRG NTWYPIFHLA PPAGWMNDPN GLIYFNGRYH AFFQHHPASA
     YQGPMHWGHA TSTDMLHWQH ELVALAPGDK YDRDGCFSGS AVDDDGVLSL IYTGHICLED
     RGNDSIIREV QCLATSHDGI RFEKQGCVLT PPEGIMHFRD PKVWHEDGSW WMVIGARDAS
     DNGQVLLYRG TSLRDWHLEH VLAHSAAGES YMWECPDFFR CGNFHWLMFS PQGMNPSGYR
     FRNLFQSGVL AGNWKPGSVF ALKGVFEELD YGHDFYAPQS MLAEDGRRII MAWMNMWDSP
     VPTRSEAWAG CLTLPREVFE RDGRLCQRPV REVESLRRKC QPLSPVRLHG VQLLTENVQA
     AELLVTWHTV DSHAEHYGIR LGEGLRFYVD NQAGRLILWR YYPEEGLDGY RSVELPDTEY
     LTLRIFLDRS SVEVFVNDGE ATLSSRIYPQ ADSRQLSLYA AHGDAILTDG TLWMLT
 
 
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