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Database: UniProt
Entry: A0A1H6WXK4_9FIRM
LinkDB: A0A1H6WXK4_9FIRM
Original site: A0A1H6WXK4_9FIRM 
ID   A0A1H6WXK4_9FIRM        Unreviewed;       508 AA.
AC   A0A1H6WXK4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=SAMN02910453_2299 {ECO:0000313|EMBL:SEJ17520.1};
OS   Lachnospiraceae bacterium A10.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1520821 {ECO:0000313|EMBL:SEJ17520.1, ECO:0000313|Proteomes:UP000198998};
RN   [1] {ECO:0000313|EMBL:SEJ17520.1, ECO:0000313|Proteomes:UP000198998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A10 {ECO:0000313|EMBL:SEJ17520.1,
RC   ECO:0000313|Proteomes:UP000198998};
RA   de Groot N.N.;
RL   Submitted (OCT-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|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}.
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DR   EMBL; FNYN01000007; SEJ17520.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6WXK4; -.
DR   OrthoDB; 9759709at2; -.
DR   UniPathway; UPA00238; -.
DR   Proteomes; UP000198998; 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:UP000198998}.
FT   DOMAIN          29..339
FT                   /note="Glycosyl hydrolase family 32 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00251"
FT   DOMAIN          342..496
FT                   /note="Glycosyl hydrolase family 32 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08244"
SQ   SEQUENCE   508 AA;  58627 MW;  9F41740C289E8809 CRC64;
     MNSQTLREAR KYEEAFEKLI PAEQRPKFHL SPRVGWMNDP NGFCIYKDKY HLFYQYHPYD
     AHWGPMHWGH AESEDLLHWK FLPVALAPDE FYDKDGVFSG SAITLKDGRH LLIYTGVMKR
     TVENGQMKEF QTQCVAIGDG LDYEKYENNP VINTDAIPEG ASKTDFRDPK IWEKADGTYR
     CLVANRPADG SGQLLLFKSN DCIHWDFVKV FAENKNRYGL MWECPDFFTL DGKGVLLTSP
     QDMLPEGFEF HNGNGNICII GSYDDDTETF TEESVQAVDY GIDFYAMQTI EMLDGRRVMI
     GWMQNWDTTG AHDGSEPWFG QMSLPREISI RDGRLCQWPI KEVEDMRSNK VEYKEVVVEA
     TRDLKASDSE LVKGGVSFEG IKGRCVDLEL EVKPKKFDEM FDQFVISIAA DEKFHTDIVL
     RPKENIAKID RKFSGSRRAI VHQRRAHIPW KSESIKMRIV MDRYSMEVFF EDGKYVMTAS
     LPTDVSCDGI YFNTNEDAVL NITKYDLN
//
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