BFRA_THEMA
ID BFRA_THEMA Reviewed; 432 AA.
AC O33833;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Beta-fructosidase;
DE EC=3.2.1.26;
DE AltName: Full=Invertase;
DE AltName: Full=Sucrase;
GN Name=bfrA; OrderedLocusNames=TM_1414;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=9720201; DOI=10.1007/s002530051256;
RA Liebl W., Brem D., Gotschlich A.;
RT "Analysis of the gene for beta-fructosidase (invertase, inulinase) of the
RT hyperthermophilic bacterium Thermotoga maritima, and characterisation of
RT the enzyme expressed in Escherichia coli.";
RL Appl. Microbiol. Biotechnol. 50:55-64(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-432.
RX PubMed=14973124; DOI=10.1074/jbc.m313911200;
RA Alberto F., Bignon C., Sulzenbacher G., Henrissat B., Czjzek M.;
RT "The three-dimensional structure of invertase (beta-fructosidase) from
RT Thermotoga maritima reveals a bimodular arrangement and an evolutionary
RT relationship between retaining and inverting glycosidases.";
RL J. Biol. Chem. 279:18903-18910(2004).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.87 ANGSTROMS) OF 2-432 IN COMPLEX WITH SUBSTRATES,
RP AND MUTAGENESIS OF GLU-190.
RX PubMed=16411890; DOI=10.1042/bj20051936;
RA Alberto F., Jordi E., Henrissat B., Czjzek M.;
RT "Crystal structure of inactivated Thermotoga maritima invertase in complex
RT with the trisaccharide substrate raffinose.";
RL Biochem. J. 395:457-462(2006).
CC -!- FUNCTION: Hydrolysis of sucrose, raffinose, inulin and levan. Specific
CC for the fructose moiety and the beta-anomeric configuration of the
CC glycosidic linkages of its substrates. The enzyme released fructose
CC from sucrose and raffinose, and the fructose polymer inulin is
CC hydrolyzed quantitatively in an exo-type fashion.
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:0000255|PROSITE-ProRule:PRU10067};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Optimum temperature is 90-95 degrees Celsius. Highly thermostable.;
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 32 family. {ECO:0000305}.
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DR EMBL; AJ001073; CAA04518.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD36485.1; -; Genomic_DNA.
DR PIR; D72255; D72255.
DR RefSeq; NP_229215.1; NC_000853.1.
DR RefSeq; WP_004081649.1; NZ_CP011107.1.
DR PDB; 1UYP; X-ray; 1.90 A; A/B/C/D/E/F=2-432.
DR PDB; 1W2T; X-ray; 1.87 A; A/B/C/D/E/F=2-432.
DR PDBsum; 1UYP; -.
DR PDBsum; 1W2T; -.
DR AlphaFoldDB; O33833; -.
DR SMR; O33833; -.
DR STRING; 243274.THEMA_07250; -.
DR DrugBank; DB04272; Citric acid.
DR CAZy; GH32; Glycoside Hydrolase Family 32.
DR PRIDE; O33833; -.
DR EnsemblBacteria; AAD36485; AAD36485; TM_1414.
DR KEGG; tma:TM1414; -.
DR eggNOG; COG1621; Bacteria.
DR InParanoid; O33833; -.
DR OMA; WMGVPDG; -.
DR OrthoDB; 1622507at2; -.
DR BRENDA; 3.2.1.26; 6331.
DR EvolutionaryTrace; O33833; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0004564; F:beta-fructofuranosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001362; Glyco_hydro_32.
DR InterPro; IPR018053; Glyco_hydro_32_AS.
DR InterPro; IPR013189; Glyco_hydro_32_C.
DR InterPro; IPR013148; Glyco_hydro_32_N.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR Pfam; PF08244; Glyco_hydro_32C; 1.
DR Pfam; PF00251; Glyco_hydro_32N; 1.
DR SMART; SM00640; Glyco_32; 1.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
DR PROSITE; PS00609; GLYCOSYL_HYDROL_F32; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..432
FT /note="Beta-fructosidase"
FT /id="PRO_0000169881"
FT ACT_SITE 17
FT BINDING 14..17
FT /ligand="substrate"
FT BINDING 33
FT /ligand="substrate"
FT BINDING 41
FT /ligand="substrate"
FT BINDING 74..75
FT /ligand="substrate"
FT BINDING 92
FT /ligand="substrate"
FT BINDING 137..138
FT /ligand="substrate"
FT BINDING 188..190
FT /ligand="substrate"
FT BINDING 208
FT /ligand="substrate"
FT BINDING 260
FT /ligand="substrate"
FT MUTAGEN 190
FT /note="E->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:16411890"
FT MUTAGEN 190
FT /note="E->D: Reduced activity."
FT /evidence="ECO:0000269|PubMed:16411890"
FT STRAND 5..7
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 11..24
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 38..40
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 45..56
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 71..81
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 84..93
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 102..114
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 133..143
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 145..156
FT /evidence="ECO:0007829|PDB:1W2T"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 160..173
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 175..183
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 190..197
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:1W2T"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 212..221
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 224..233
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 249..258
FT /evidence="ECO:0007829|PDB:1W2T"
FT TURN 260..262
FT /evidence="ECO:0007829|PDB:1W2T"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:1W2T"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 281..286
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 289..294
FT /evidence="ECO:0007829|PDB:1W2T"
FT HELIX 296..301
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 302..311
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 324..339
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 344..350
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 377..386
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 389..394
FT /evidence="ECO:0007829|PDB:1W2T"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 398..403
FT /evidence="ECO:0007829|PDB:1W2T"
FT STRAND 412..427
FT /evidence="ECO:0007829|PDB:1W2T"
SQ SEQUENCE 432 AA; 49841 MW; 39F61B2E1BC462B9 CRC64;
MFKPNYHFFP ITGWMNDPNG LIFWKGKYHM FYQYNPRKPE WGNICWGHAV SDDLVHWRHL
PVALYPDDET HGVFSGSAVE KDGKMFLVYT YYRDPTHNKG EKETQCVAMS ENGLDFVKYD
GNPVISKPPE EGTHAFRDPK VNRSNGEWRM VLGSGKDEKI GRVLLYTSDD LFHWKYEGVI
FEDETTKEIE CPDLVRIGEK DILIYSITST NSVLFSMGEL KEGKLNVEKR GLLDHGTDFY
AAQTFFGTDR VVVIGWLQSW LRTGLYPTKR EGWNGVMSLP RELYVENNEL KVKPVDELLA
LRKRKVFETA KSGTFLLDVK ENSYEIVCEF SGEIELRMGN ESEEVVITKS RDELIVDTTR
SGVSGGEVRK STVEDEATNR IRAFLDSCSV EFFFNDSIAF SFRIHPENVY NILSVKSNQV
KLEVFELENI WL
