ID H4GK80_9LACO Unreviewed; 472 AA.
AC H4GK80;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE RecName: Full=Sucrose-6-phosphate hydrolase {ECO:0000256|ARBA:ARBA00019623, ECO:0000256|RuleBase:RU362110};
DE EC=3.2.1.26 {ECO:0000256|ARBA:ARBA00012758, ECO:0000256|RuleBase:RU362110};
DE AltName: Full=Invertase {ECO:0000256|ARBA:ARBA00033367, ECO:0000256|RuleBase:RU365015};
GN ORFNames=PS3_16953 {ECO:0000313|EMBL:EHS85532.1};
OS Limosilactobacillus gastricus PS3.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=1144300 {ECO:0000313|EMBL:EHS85532.1, ECO:0000313|Proteomes:UP000004567};
RN [1] {ECO:0000313|EMBL:EHS85532.1, ECO:0000313|Proteomes:UP000004567}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PS3 {ECO:0000313|EMBL:EHS85532.1,
RC ECO:0000313|Proteomes:UP000004567};
RX PubMed=23846278;
RA Martin V., Cardenas N., Jimenez E., Maldonado A., Rodriguez J.M.,
RA Fernandez L.;
RT "Genome Sequence of Lactobacillus gastricus PS3, a Strain Isolated from
RT Human Milk.";
RL Genome Announc. 1:E00489-E00413(2013).
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|ARBA:ARBA00004914, 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:EHS85532.1}.
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DR EMBL; AICN01000062; EHS85532.1; -; Genomic_DNA.
DR RefSeq; WP_007122463.1; NZ_AICN01000062.1.
DR AlphaFoldDB; H4GK80; -.
DR STRING; 1144300.PS3_16953; -.
DR PATRIC; fig|1144300.3.peg.1338; -.
DR OrthoDB; 9759709at2; -.
DR UniPathway; UPA00238; -.
DR Proteomes; UP000004567; 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; 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.
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:UP000004567}.
FT DOMAIN 22..324
FT /note="Glycosyl hydrolase family 32 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00251"
FT DOMAIN 331..448
FT /note="Glycosyl hydrolase family 32 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08244"
SQ SEQUENCE 472 AA; 53985 MW; 4A3CE3C08C623212 CRC64;
MSLVKAKEPI TVTNARYRQH YHLQTPGGWL NDPNGLCYFQ GYYHVFYQYH PYSAEWGPMH
WGHARSQDLL HWEDLPMALT PGDPEDTGGC FSGSAIVKDN RLYLIYTGHH YYDDGDQDHF
WENQNVAYSD DGIHFTKYAG NPVIEAPDDN GQDFRDPKVW AHDGQYYLIV GSQAQPSRTG
RVLLYQSADL FNWQLLGPIT IAQSIDSEGF MWECPDLFHL NGQDTLVFSP MGIAAQGHDF
LNLNQVASVM GNLDYSHHAL NRGSLYEIDH GHNFYAPQSF LAPDGRQMMY GWMSSFDDPY
PEQADGWCGC LTVPREYVIK NHHLGMIPVA ELAQLRQQTI VSETIQLNHP VTIAYNDAQH
AELDLTLEHP QNYQWRFRNQ DQVIMSLTFD PEQNEFNLDR PHHGGKRYVT ITPQPTHHLQ
IIIDTSSVEI FINDGEACFT ERYYIDEAPS VILSAREPTK AQLAAYQLGI PD
//
