ID A0A0Q9U1G9_9BACL Unreviewed; 1348 AA.
AC A0A0Q9U1G9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=beta-fructofuranosidase {ECO:0000256|ARBA:ARBA00012758};
DE EC=3.2.1.26 {ECO:0000256|ARBA:ARBA00012758};
GN ORFNames=ASG93_20135 {ECO:0000313|EMBL:KRF43020.1};
OS Paenibacillus sp. Soil787.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1736411 {ECO:0000313|EMBL:KRF43020.1, ECO:0000313|Proteomes:UP000051948};
RN [1] {ECO:0000313|EMBL:KRF43020.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF43020.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRF43020.1, ECO:0000313|Proteomes:UP000051948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil787 {ECO:0000313|EMBL:KRF43020.1,
RC ECO:0000313|Proteomes:UP000051948};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family.
CC {ECO:0000256|ARBA:ARBA00009902}.
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:KRF43020.1}.
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DR EMBL; LMSP01000002; KRF43020.1; -; Genomic_DNA.
DR STRING; 1736411.ASG93_20135; -.
DR Proteomes; UP000051948; Unassembled WGS sequence.
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 Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR InterPro; IPR003343; Big_2.
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; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR006558; LamG-like.
DR PANTHER; PTHR43101; BETA-FRUCTOSIDASE; 1.
DR PANTHER; PTHR43101:SF1; BETA-FRUCTOSIDASE; 1.
DR Pfam; PF02368; Big_2; 1.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR SMART; SM00635; BID_2; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SMART; SM00560; LamGL; 1.
DR SUPFAM; SSF75005; Arabinanase/levansucrase/invertase; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 99..253
FT /note="LamG-like jellyroll fold"
FT /evidence="ECO:0000259|SMART:SM00560"
FT DOMAIN 780..856
FT /note="BIG2"
FT /evidence="ECO:0000259|SMART:SM00635"
SQ SEQUENCE 1348 AA; 147350 MW; 5E57A4BA1B2F8CB9 CRC64;
MKWLQLRVLF FTMVIFTSSI VINSPVSKAV SSVVAQWSFN EGTGNVTKEL ISQISDPIHY
FKPAPAIPEW KTDGISSSAL LFDGYSTWVS HPAISIPQSK ISVETWVAPR AYTWGDDFKL
DAIVNQQSKS ANQGFLLGMY RYGTWSFQFG SNGTWYDVWS YEPLPKFEWS HIVATYDSAY
DNTGGLAVLY LNGKQVASKR TPLNTLITSS ANNLLIGTNN ESTYGASPSL FPYHTFNGLI
DELKIYNGAL TATEVQNSYN SQLTNLDGNL PTPNLSFDRS VYNGDNYRPT YHAIAPQHWM
NEPHAPLFFN GQYHMFYQFN QQGPYWHNMH WGHWVSTDMV HWRDLPPALA PSLFQVDPDG
DWTGGSVIDD SGNPALFFTA GNDAKAPNNE NVGLARSTYP TDQDNDLKRW DKDASLAVTQ
QAGQGIQGEF RDPFVFKDGS TWNMLVGSGI SGQGGTALVY TSSDMTNWQY KGPLYQNNLY
PAELGNVWEL PVLLPIKDSL GRQKYIFMVS PIGGQVRVYY WIGTWNNVTS QFTPDPGSDA
PQLMDYGGFH FTGPSGFVDK STSAYNTPNR TILNTIAQGN RNSQADSDAG WAHNAGLPVA
LDLRLDGQLG INPISELQSL RGTQLVDITT DTSFTDANQI LSRLQGDTLE IDMELSPGTA
DKVGMYVRKS PTSGEKTLLY YKKSTKEYGV DRTNTIAGQP QGIDSGTIDL AGDDTVKLHI
FLDKSMVESY LNGLKSITTR TYSTSNDALG LQLFGDVNPD TITVKHLQIW NMNSAYTPVP
VTGVSLNTES SQVFTGGKQT LYATVAPSNA TNKDIVWTSS NSAVATVTNG SVSGNSVGTA
IITAKTRDGG FLATSTVTVV APPASTPLTN GNFEAGNLSN WTVVSGNEFT DHAVVTKSPT
WWGVQPFNQQ GAFHLWGSNG AEGDSPIGEL RSQTFTLGGN GQINFLVGGG IDIDNLYVAF
VRSSDGKELY RTSGPGTYKD WADHKGDTEQ YTRRYWDATP YIGTSMYIRV VDNRSDSWGH
INVDDFNIPI QATEQLPNYN FEAGNLSGWI VESGNAFTDA DVSSASTFWS PPQSFNKEGD
YHFWGFNNGG DDRVGAMRSV SFVLGGNGLI NLRVGGGQDI NNLYVALVRA SDNAILFKET
GLNNEGYTVS NWDASAYIGT RCYIRVVDNS TGGFGHINLD AVNVPVQAGS MIGQLANHDF
ELGNLSGWNV TSGNAFTDSD VSSASTFWNP PQSFNKQGTY HYWGFNNGGD GRVGSMQSTN
FVLGGDGQID LLVGGGQDLN NLYVALVRAS DNAILFKETG LNNEAYTRKN WNASTYIGTT
CYIKMVDNTM GGFGHINIDD VNVPIRIP
//
