ID Q3YZG7_SHISS Unreviewed; 477 AA.
AC Q3YZG7;
DT 27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Sucrose-6-phosphate hydrolase {ECO:0000256|RuleBase:RU362110};
DE EC=3.2.1.26 {ECO:0000256|RuleBase:RU362110};
DE AltName: Full=Invertase {ECO:0000256|RuleBase:RU365015};
GN OrderedLocusNames=SSON_2454 {ECO:0000313|EMBL:AAZ89095.1};
OS Shigella sonnei (strain Ss046).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269 {ECO:0000313|EMBL:AAZ89095.1, ECO:0000313|Proteomes:UP000002529};
RN [1] {ECO:0000313|EMBL:AAZ89095.1, ECO:0000313|Proteomes:UP000002529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046 {ECO:0000313|EMBL:AAZ89095.1,
RC ECO:0000313|Proteomes:UP000002529};
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
CC -!- FUNCTION: Enables the bacterium to metabolize sucrose as a sole carbon
CC source. {ECO:0000256|RuleBase:RU365015}.
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:0000256|RuleBase:RU362110};
CC -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC {ECO:0000256|RuleBase:RU365015}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU365015}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family.
CC {ECO:0000256|ARBA:ARBA00009902, ECO:0000256|RuleBase:RU362110}.
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DR EMBL; CP000038; AAZ89095.1; -; Genomic_DNA.
DR RefSeq; WP_000194509.1; NC_007384.1.
DR AlphaFoldDB; Q3YZG7; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR KEGG; ssn:SSON_2454; -.
DR HOGENOM; CLU_001528_7_0_6; -.
DR UniPathway; UPA00238; -.
DR Proteomes; UP000002529; 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 CDD; cd08996; GH32_FFase; 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 NCBIfam; TIGR01322; scrB_fam; 1.
DR PANTHER; PTHR43101; BETA-FRUCTOSIDASE; 1.
DR PANTHER; PTHR43101:SF1; BETA-FRUCTOSIDASE; 1.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU365015};
KW Cytoplasm {ECO:0000256|RuleBase:RU365015};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU362110};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362110};
KW Reference proteome {ECO:0000313|Proteomes:UP000002529}.
FT DOMAIN 29..330
FT /note="Glycosyl hydrolase family 32 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00251"
FT DOMAIN 333..471
FT /note="Glycosyl hydrolase family 32 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08244"
SQ SEQUENCE 477 AA; 54460 MW; 64B345F345C031FA CRC64;
MTQSRLHAAQ NALAKLHEHR GNTFYPHFHL APPAGWMNDP NGLIWFNDRY HAFYQHHPMS
EHWGPMHWGH ATSDDMIHWQ HEPIALAPGD DNDKDGCFSG SAVDDNGVLS LIYTGHVWLD
CAGNDDAIRE VQCLATSRDG IHFEKQGVIL TPPEGIMHFR DPKVWREADT WWMVVGAKDP
GNTGQILLYR GSSLREWTFD RVLAHADAGE SYMWECPDFF SLGDQHYLMF SPQGMNAEGY
SYRNRFQSGV IPGMWSPGRL FAQSGHFTEL DNGHDFYAPQ SFLAKDGRRI VIGWMDMWES
PMPSKREGWA GCMTLARELS ESNGKLLQRP VHEAESLRQQ HQSVSPRTIS NKYVLQENAQ
AVEIQLQWAL KNSDAEHYGL QLGTGMRLYI DNQSERLVLW RYYPHENLDG YRSIPLPQRD
TLALRIFIDT SSVEVFINDG EAVMSSRIYP QPEERELSLY ASHGVAVLQH GALWLLG
//
