ID B3DQ70_BIFLD Unreviewed; 518 AA.
AC B3DQ70;
DT 22-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE RecName: Full=beta-fructofuranosidase {ECO:0000256|ARBA:ARBA00012758};
DE EC=3.2.1.26 {ECO:0000256|ARBA:ARBA00012758};
GN Name=sacA {ECO:0000313|EMBL:ACD97569.1};
GN OrderedLocusNames=BLD_0123 {ECO:0000313|EMBL:ACD97569.1};
OS Bifidobacterium longum (strain DJO10A).
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=205913 {ECO:0000313|EMBL:ACD97569.1, ECO:0000313|Proteomes:UP000002419};
RN [1] {ECO:0000313|EMBL:ACD97569.1, ECO:0000313|Proteomes:UP000002419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJO10A {ECO:0000313|EMBL:ACD97569.1,
RC ECO:0000313|Proteomes:UP000002419};
RX PubMed=16391088; DOI=10.1128/AEM.72.1.527-535.2006;
RA Lee J.H., O'Sullivan D.J.;
RT "Sequence analysis of two cryptic plasmids from Bifidobacterium longum
RT DJO10A and construction of a shuttle cloning vector.";
RL Appl. Environ. Microbiol. 72:527-535(2006).
RN [2] {ECO:0000313|EMBL:ACD97569.1, ECO:0000313|Proteomes:UP000002419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJO10A {ECO:0000313|EMBL:ACD97569.1,
RC ECO:0000313|Proteomes:UP000002419};
RX PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT reveals loci susceptible to deletion during pure culture growth.";
RL BMC Genomics 9:247-247(2008).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family.
CC {ECO:0000256|ARBA:ARBA00009902, ECO:0000256|RuleBase:RU362110}.
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DR EMBL; CP000605; ACD97569.1; -; Genomic_DNA.
DR RefSeq; WP_007054055.1; NC_010816.1.
DR AlphaFoldDB; B3DQ70; -.
DR SMR; B3DQ70; -.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR KEGG; blj:BLD_0123; -.
DR HOGENOM; CLU_001528_7_0_11; -.
DR OMA; WMGVPDG; -.
DR Proteomes; UP000002419; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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 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 Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU362110};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362110}.
FT DOMAIN 44..354
FT /note="Glycosyl hydrolase family 32 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00251"
FT DOMAIN 358..510
FT /note="Glycosyl hydrolase family 32 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08244"
SQ SEQUENCE 518 AA; 58091 MW; F203700772422F49 CRC64;
MTDFTPETPV LTPIRDHAAE LAKAEAGVAE MAAKRNNRWY PKYHIASNGG WINDPNGLCF
YKGRWHVFYQ LHPYGTQWGP MHWGHVSSTD MLNWKREPIM FAPSLEQEKD GVFSGSAVID
DNGDLRFYYT GHRWANGHDN TGGDWQVQMT ALPDNDELTS ATKQGMIIDC PTDKVDHHYR
DPKVWKTGDT WYMTFGVSSA DKRGQMWLFS SKDMVRWEYE RVLFQHPDPD VFMLECPDFF
PIKDKDGNEK WVIGFSAMGS KPSGFMNRNV SNAGYMIGTW EPGGEFKPET EFRLWDCGHN
YYAPQSFNVD GRQIVYGWMS PFVQPIPMED DGWCGQLTLP REITLGDDGD VVTAPVAEME
GLREDTLDHG SVTLDMDGEQ IIADDAEAVE IEMTIDLAAS TAERAGLKIH ATEDGAYTYV
AYDGQIGRVV VDRQAMANGD RGYRAAPLTD AELASGKLDL RVFVDRGSVE VYVNGGHQVL
SSYSYASEGP RAIKLVAESG SLKVDSLKLH HMKSIGLE
//