ID A0A1V2SQW4_9STRE Unreviewed; 484 AA.
AC A0A1V2SQW4;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-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=BVE84_00425 {ECO:0000313|EMBL:ONK31018.1};
OS Streptococcus azizii.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1579424 {ECO:0000313|EMBL:ONK31018.1, ECO:0000313|Proteomes:UP000188946};
RN [1] {ECO:0000313|EMBL:ONK31018.1, ECO:0000313|Proteomes:UP000188946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12-5202 {ECO:0000313|EMBL:ONK31018.1,
RC ECO:0000313|Proteomes:UP000188946};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-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}.
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:ONK31018.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MSPR01000001; ONK31018.1; -; Genomic_DNA.
DR RefSeq; WP_076995124.1; NZ_MSPT01000006.1.
DR AlphaFoldDB; A0A1V2SQW4; -.
DR STRING; 1579424.BVE84_00425; -.
DR OrthoDB; 9759709at2; -.
DR UniPathway; UPA00238; -.
DR Proteomes; UP000188946; 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; 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}.
FT DOMAIN 37..340
FT /note="Glycosyl hydrolase family 32 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00251"
FT DOMAIN 358..470
FT /note="Glycosyl hydrolase family 32 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08244"
SQ SEQUENCE 484 AA; 54999 MW; E0EADB204235690E CRC64;
MAFTTEERYR AYADWPADHI ETIKQNTKSS PWRTNFHIET PHGLLNDPNG FSHFNGKWTL
FYQYFPFGAA HGLKSWVHME SADLVHFEKT GTILYPDTAL DSHGAYSGSA MQFDDHLFLF
YTGNVRDENW VRHPYQIGAL MDTDGHIQKL NKVLIDQPSD TTDHFRDPQI FNYEGNYYAI
VGGQNLEKQG IIKLYKAVNN DYLNWEYIDD LAFDNDLTAY MMECPNLVFI SGQPVLLYCP
QGLDKTVLDY GNIYPNLYKV GQSFNPETAT MINPGPLEQL DYGFECYATQ AFNDPFGRAL
AVSWLALPDV DYPTDRYDYQ GCLSLVKELT IKDGKLYQYP VPAITSLRAE AQLFTEKTKT
DNTYELELTI EANSHLELVL FADADGHGLK LTIDPTNGCI VLDRKDCGEA FALDFGTTRH
CQIANQATIA NIFIDKSVFE IFINKGEKVF SGRVFPRQDQ SGITILSGQA TGNYYPLDYG
HKTH
//
