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