ID A0A1E3L1J4_9BACL Unreviewed; 490 AA.
AC A0A1E3L1J4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=PTI45_03029 {ECO:0000313|EMBL:ODP27574.1};
OS Paenibacillus nuruki.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1886670 {ECO:0000313|EMBL:ODP27574.1, ECO:0000313|Proteomes:UP000094578};
RN [1] {ECO:0000313|EMBL:ODP27574.1, ECO:0000313|Proteomes:UP000094578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TI45-13ar {ECO:0000313|EMBL:ODP27574.1,
RC ECO:0000313|Proteomes:UP000094578};
RA Kim S.-J.;
RT "Genome sequencing of Paenibacillus sp. TI45-13ar, isolated from Korean
RT traditional nuruk.";
RL Submitted (AUG-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:ODP27574.1}.
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; MDER01000051; ODP27574.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3L1J4; -.
DR STRING; 1886670.PTI45_03029; -.
DR PATRIC; fig|1886670.3.peg.3077; -.
DR UniPathway; UPA00238; -.
DR Proteomes; UP000094578; 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:UP000094578}.
FT DOMAIN 28..336
FT /note="Glycosyl hydrolase family 32 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00251"
FT DOMAIN 340..483
FT /note="Glycosyl hydrolase family 32 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08244"
SQ SEQUENCE 490 AA; 56406 MW; 95E3DA0276F692A7 CRC64;
MSYSIERANH FVAESKHLLV DQYRLHYHFM GEFGWINDPN GFVQYKGEYH LFYQYHPYQP
VWGPMHWGHA VSKDLIEWRH LPVALAPDQE YDRDGCFSGS AIEHNDSLYL LYTGHIMTGP
DITKDYYQVQ NLAISQDGIL FTKDAHNPVI NTDQIPAHTS QKDFRDPKVF ERNGQFYMVL
GSNDDQGKGL ILLYRSVDLH TWEYMNVMAQ SDGTLGDNWE CPDVFDLDGI DVLMMSPQRM
SPQGNNYHNL HSTVYMLGKL DTDTGIFDYK QYIPIDYGFD FYACQTTLDQ QGRRIMIGWM
DSWEALMPTQ NGHHWAGAMT LPREVIRDGE RLLFRPVAEL EQSRLEGLHA ESFEVQGQQV
LDYRGESYEI ELNVDVSKSE EFAIHLRTGE AETTVLSYSP LEQLFRFNRD QSGIGPGGER
ITSLTTSEGQ LHLRIFVDLS SVEVFLQDGE KVMTGRIYPQ PESQGIALYS NGITQVQSLH
IWNLVQPEQI
//
