ID A0A1B8TWT6_9FLAO Unreviewed; 699 AA.
AC A0A1B8TWT6;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=beta-fructofuranosidase {ECO:0000256|ARBA:ARBA00012758};
DE EC=3.2.1.26 {ECO:0000256|ARBA:ARBA00012758};
GN ORFNames=LPB3_06525 {ECO:0000313|EMBL:OBY64052.1};
OS Polaribacter vadi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1774273 {ECO:0000313|EMBL:OBY64052.1, ECO:0000313|Proteomes:UP000092584};
RN [1] {ECO:0000313|Proteomes:UP000092584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0003 {ECO:0000313|Proteomes:UP000092584};
RA Shin S.-K., Yi H., Kim E.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00000094};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 100 family.
CC {ECO:0000256|ARBA:ARBA00007671}.
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:OBY64052.1}.
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DR EMBL; LSFM01000022; OBY64052.1; -; Genomic_DNA.
DR RefSeq; WP_065318804.1; NZ_LSFM01000022.1.
DR AlphaFoldDB; A0A1B8TWT6; -.
DR STRING; 1774273.LPB03_05965; -.
DR KEGG; pob:LPB03_05965; -.
DR OrthoDB; 49490at2; -.
DR Proteomes; UP000092584; Unassembled WGS sequence.
DR GO; GO:0033926; F:glycopeptide alpha-N-acetylgalactosaminidase activity; IEA:InterPro.
DR GO; GO:0016791; F:phosphatase activity; IEA:UniProt.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 3.90.1070.10; -; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR024746; Glyco_hydro_100.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006380; SPP-like_dom.
DR NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR PANTHER; PTHR46521:SF16; S6PP DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46521; SUCROSE-PHOSPHATASE 2-RELATED; 1.
DR Pfam; PF12899; Glyco_hydro_100; 1.
DR Pfam; PF05116; S6PP; 1.
DR SFLD; SFLDG01141; C2.B.1:_Sucrose_Phosphatase_Li; 1.
DR SFLD; SFLDG01140; C2.B:_Phosphomannomutase_and_P; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 3: Inferred from homology;
FT DOMAIN 13..253
FT /note="Sucrose phosphatase-like"
FT /evidence="ECO:0000259|Pfam:PF05116"
SQ SEQUENCE 699 AA; 79632 MW; 307AFA08C42707D7 CRC64;
MKNKNLKKEN RIKLLSFDID NTLIDFHTYK SNFTKTWVKY AKDLDIIITY NTGRLIDDVL
NLINKGVLPK PDYIISGVGT HIYNYEEGKV VKEFNDVLDD GWNLKAVENI INKINHPISQ
QPSKFQHSYK RSYFFHDATD ELVESVAQDF SNANMDVNVI YSGDKFLDVL PKWANKGNAL
QWLLKRLTLE TNQVLVAGDS GNDSAMFDLK DVSGIVVANA HEELYKYTKH KKVYHTEKAK
GDGIIEGLIF YGILPKEASE ISNIDHTEDF FIKKELDNIA DEDDSEKIEL IQEGYKKAIE
ALRKNITPLG FSACSIPDNI PNGTDENYHS VWARDGAITV IGSLSLIDDE EIHKCQRQTL
ETLLGHISRN GQIPSNVRLK DNEPDYSGVG GICSIDSGIW VVIAFYEYVN VTKDIEFARK
YIGDIKETMR WLGAHDSNND ALLEIPEAGD WTDLFGRSYN ILYDEILWYR SNVCFGRLLE
MLGNHEEAGE YIRWSQVIKK EIVQNFWPST QQQLFSSVSF AEKQFTLGDT SYLIAQTTPF
DFSWRCDTLG NVLAFLHGTI DSEKAHQTFK FMLGVGVNDP FPIANVYPVV SPGDPDWRPY
YTVNLLNLPN HYHNGGIWPF VGGFWVKYVN KLGFRDIAIA ELHKLALINK EGINNEWEFT
EWAHGVTGKP MGKAYQAWSA AQYIAACHDL KLTNMNTKK
//
