ID A0A1B7JMH4_9GAMM Unreviewed; 484 AA.
AC A0A1B7JMH4;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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 ORFNames=M998_3083 {ECO:0000313|EMBL:OAT49107.1};
OS Providencia heimbachae ATCC 35613.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1354272 {ECO:0000313|EMBL:OAT49107.1, ECO:0000313|Proteomes:UP000078224};
RN [1] {ECO:0000313|EMBL:OAT49107.1, ECO:0000313|Proteomes:UP000078224}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35613 {ECO:0000313|EMBL:OAT49107.1,
RC ECO:0000313|Proteomes:UP000078224};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OAT49107.1}.
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DR EMBL; LXEW01000042; OAT49107.1; -; Genomic_DNA.
DR RefSeq; WP_068909673.1; NZ_LXEW01000042.1.
DR AlphaFoldDB; A0A1B7JMH4; -.
DR GeneID; 79027076; -.
DR PATRIC; fig|1354272.4.peg.3145; -.
DR OrthoDB; 9801455at2; -.
DR UniPathway; UPA00238; -.
DR Proteomes; UP000078224; Unassembled WGS sequence.
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:UP000078224}.
FT DOMAIN 28..331
FT /note="Glycosyl hydrolase family 32 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00251"
FT DOMAIN 334..477
FT /note="Glycosyl hydrolase family 32 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08244"
SQ SEQUENCE 484 AA; 56111 MW; 9FCDC87A64EE3936 CRC64;
MKQRIELATN AIKKARKSLN KQFYPHYHLA PYAGWLNDPN GLIYHDGLYH AFYQHHPFSS
LWGPMHWGHA TSEDMIHWQH QPIALAPGDE YDKDGCFSGS AVSHEGKLYL FYTGHIWLNG
ANDDSAIHQT QCVAISDDGI HFEKKGVVIP SPEGFMHFRD PKVWFQDGKW WMVVGARDAL
DQGQILLFST TDLLNWNDEY QTLAKTEDKN VYMWECPDFF PLGNHFITLF SPQGKKSQDY
QFRNLYQNGY LVGQWAPDQP YEITHQFSEL DFGQDFYAPQ TFLAKDGRRI AMAWMDMWES
HMPSQEHGWS GCFTLPRELV LNDQGKIIAN PIEELKTLRQ DEKIIPSTIL IKNTDILINE
NATCCELELV WDLQNSSAEK FGFWIGNGIQ FYIDNQNQKL TLSRHYPKYI ISDSRSTELP
KTKQLKIRAF IDKSSLEVFI NDGEQTFSCR IYPQDSDYTL KLFAINQSAK LDNGTFWNLE
RAIS
//
