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Database: UniProt
Entry: A0A1Y4MCS8_9FIRM
LinkDB: A0A1Y4MCS8_9FIRM
Original site: A0A1Y4MCS8_9FIRM 
ID   A0A1Y4MCS8_9FIRM        Unreviewed;       466 AA.
AC   A0A1Y4MCS8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=B5F12_05460 {ECO:0000313|EMBL:OUP64492.1};
OS   Pseudoflavonifractor sp. An176.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Pseudoflavonifractor.
OX   NCBI_TaxID=1965572 {ECO:0000313|EMBL:OUP64492.1, ECO:0000313|Proteomes:UP000196146};
RN   [1] {ECO:0000313|Proteomes:UP000196146}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An176 {ECO:0000313|Proteomes:UP000196146};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) 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}.
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:OUP64492.1}.
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DR   EMBL; NFKO01000007; OUP64492.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4MCS8; -.
DR   UniPathway; UPA00238; -.
DR   Proteomes; UP000196146; 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; cd18623; GH32_ScrB-like; 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:UP000196146}.
FT   DOMAIN          34..338
FT                   /note="Glycosyl hydrolase family 32 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00251"
FT   DOMAIN          410..446
FT                   /note="Glycosyl hydrolase family 32 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08244"
SQ   SEQUENCE   466 AA;  52883 MW;  918D93FFA8E7CBA7 CRC64;
     MSNALQRDLE RLVARVERED GPQAAADPFR QTFHLMPPVG WLNDPNGLCR CGDWYHVFYQ
     YGPFDVTGGV KHWGHYRSRD LLHWEALPVM LYPDQPWDIH GVYSGSALVE DGTLYLYYTG
     NVKHAGNYDY IKAGRGHNTA LAVSKDGVTV ESNTLLMENK DYPDGLTCHV RDPKVWAQDG
     KYYMVQGART LDDHGQLLVF ESTDKFNWTF LQALKTPHHF GYMWECPDLF CVDGQWFLVC
     SPQGVPHEET RFQNVYSCGY FPLHGDFRGE YSLGEFVEMD LGFDFYAPQT FQDGDRRLMF
     GWMGMPDADY TNPTTQRGWQ HCLTVPCELR RQGDRLVRLP AVEVTALRGA AIPAHQAQVF
     DLEAMTEPRG RMVFRDAAVL EWQPGLVTLS FLEGGAGRTL RRVAVDQLNA LRILGDRSSL
     EIFLNDGQQV LSTRYYPQPE AQGIAITGAQ ARVWEMGAMP VTQAEG
//
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