ID A0A0F4KWW8_9LACO Unreviewed; 479 AA.
AC A0A0F4KWW8;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=JG29_01300 {ECO:0000313|EMBL:KJY51087.1};
OS Bombilactobacillus mellis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Bombilactobacillus.
OX NCBI_TaxID=1218508 {ECO:0000313|EMBL:KJY51087.1, ECO:0000313|Proteomes:UP000033695};
RN [1] {ECO:0000313|EMBL:KJY51087.1, ECO:0000313|Proteomes:UP000033695}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hon2 {ECO:0000313|EMBL:KJY51087.1,
RC ECO:0000313|Proteomes:UP000033695};
RA Ellegaard K.M., Tamarit D., Javelind E., Olofsson T., Andersson S.G.,
RA Vasquez A.;
RT "Comparative genomics of the lactic acid bacteria isolated from the honey
RT bee gut.";
RL Submitted (DEC-2014) 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:KJY51087.1}.
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DR EMBL; JXBZ01000002; KJY51087.1; -; Genomic_DNA.
DR RefSeq; WP_045922045.1; NZ_KQ033877.1.
DR AlphaFoldDB; A0A0F4KWW8; -.
DR STRING; 1218508.JG29_01300; -.
DR PATRIC; fig|1218508.4.peg.134; -.
DR HOGENOM; CLU_001528_7_0_9; -.
DR OrthoDB; 9759709at2; -.
DR UniPathway; UPA00238; -.
DR Proteomes; UP000033695; 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:UP000033695}.
FT DOMAIN 18..324
FT /note="Glycosyl hydrolase family 32 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00251"
FT DOMAIN 327..446
FT /note="Glycosyl hydrolase family 32 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08244"
SQ SEQUENCE 479 AA; 55355 MW; 022943CF50729428 CRC64;
MTIAPIQVTN HRYRLGYHLM APAGWINDPN GLCYFQGYYH VFYQYHPYSA TWGPMSWGHA
RSRDLLHWQT LPIAIKPNSW TDHDGCFSGS ALIKDQGLHL LYTGNNYYNR SNVNEYWQNQ
NLAVSYDGRH FTKYLNNPVI AQPPLDNTEN FRDPKVWEYD GLYYAVIGGQ SPTGLGQLLF
YQTADLKHWH YLGILAQAQT AATEGYMWEC PDLFRLNGQD ILLISPQGIQ AQAQRYLNLY
QTGYFVGRLD YQQPALVHGS FQELDQGHDF YAAQTMLTPD GRRIMIGWLN MWDNEMLEQA
DGWAGALTLP RELVYKNEHL YQQPIAETKT LRQQVLVNKS WPTKQTVTLI QGYSQLEINL
KIDLTQVNDL NLNIKMSDPP TPNHLTLQYN QTRHQFLLYN FNRPGVRIAA LSSCPELKLQ
IFLDTSSVEI FLNDGEAVLT ERYYFQNSPL ITMTTDKAAD VQCVIYQLSS QTNNYHYEI
//
