F16PA_STRMK
ID F16PA_STRMK Reviewed; 338 AA.
AC B2FU10;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Fructose-1,6-bisphosphatase class 1 {ECO:0000255|HAMAP-Rule:MF_01855};
DE Short=FBPase class 1 {ECO:0000255|HAMAP-Rule:MF_01855};
DE EC=3.1.3.11 {ECO:0000255|HAMAP-Rule:MF_01855};
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 {ECO:0000255|HAMAP-Rule:MF_01855};
GN Name=fbp {ECO:0000255|HAMAP-Rule:MF_01855}; OrderedLocusNames=Smlt0047;
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a;
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01855};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01855};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01855};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_01855}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01855}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01855}.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family. {ECO:0000255|HAMAP-
CC Rule:MF_01855}.
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DR EMBL; AM743169; CAQ43662.1; -; Genomic_DNA.
DR RefSeq; WP_012478654.1; NC_010943.1.
DR PDB; 7K74; X-ray; 2.20 A; A/B/C/D=6-338.
DR PDBsum; 7K74; -.
DR AlphaFoldDB; B2FU10; -.
DR SMR; B2FU10; -.
DR STRING; 522373.Smlt0047; -.
DR EnsemblBacteria; CAQ43662; CAQ43662; Smlt0047.
DR KEGG; sml:Smlt0047; -.
DR PATRIC; fig|522373.3.peg.39; -.
DR eggNOG; COG0158; Bacteria.
DR HOGENOM; CLU_039977_0_0_6; -.
DR OMA; YIPENCP; -.
DR OrthoDB; 945770at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000008840; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR CDD; cd00354; FBPase; 1.
DR HAMAP; MF_01855; FBPase_class1; 1.
DR InterPro; IPR044015; FBPase_C_dom.
DR InterPro; IPR000146; FBPase_class-1.
DR InterPro; IPR033391; FBPase_N.
DR InterPro; IPR028343; FBPtase.
DR PANTHER; PTHR11556; PTHR11556; 1.
DR Pfam; PF00316; FBPase; 1.
DR Pfam; PF18913; FBPase_C; 1.
DR PIRSF; PIRSF500210; FBPtase; 1.
DR PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR PRINTS; PR00115; F16BPHPHTASE.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium;
KW Metal-binding; Reference proteome.
FT CHAIN 1..338
FT /note="Fructose-1,6-bisphosphatase class 1"
FT /id="PRO_0000364723"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 114
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 115..118
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 207
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT HELIX 6..15
FT /evidence="ECO:0007829|PDB:7K74"
FT HELIX 21..42
FT /evidence="ECO:0007829|PDB:7K74"
FT HELIX 43..47
FT /evidence="ECO:0007829|PDB:7K74"
FT HELIX 60..75
FT /evidence="ECO:0007829|PDB:7K74"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:7K74"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:7K74"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:7K74"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:7K74"
FT STRAND 106..116
FT /evidence="ECO:0007829|PDB:7K74"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:7K74"
FT TURN 120..123
FT /evidence="ECO:0007829|PDB:7K74"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:7K74"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:7K74"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:7K74"
FT STRAND 155..174
FT /evidence="ECO:0007829|PDB:7K74"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:7K74"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:7K74"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:7K74"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:7K74"
FT HELIX 208..213
FT /evidence="ECO:0007829|PDB:7K74"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:7K74"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:7K74"
FT STRAND 238..241
FT /evidence="ECO:0007829|PDB:7K74"
FT HELIX 245..255
FT /evidence="ECO:0007829|PDB:7K74"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:7K74"
FT STRAND 273..275
FT /evidence="ECO:0007829|PDB:7K74"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:7K74"
FT HELIX 280..289
FT /evidence="ECO:0007829|PDB:7K74"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:7K74"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:7K74"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:7K74"
FT STRAND 315..318
FT /evidence="ECO:0007829|PDB:7K74"
FT HELIX 320..334
FT /evidence="ECO:0007829|PDB:7K74"
SQ SEQUENCE 338 AA; 36797 MW; 81E0EDFDE3E6FFEA CRC64;
MSRTSLTRFL IQEQHAGRIN ADLRQLIAVV ARACTSISIA VSKGALGGVL GDAGTGNVQG
EAQKKLDVIS NEILLEANAW GGHLAACASE EMDHSQPVPD IYPRGDFLLL FDPLDGSSNI
DVNVSVGTIF SVLRCPTNVE LPGDDAFLQP GSKQIAAGYC IYGPSTQLVL TVGHGTHAFT
LDREKGEFVL TTENMQIPAA TQEFAINMSN QRHWEAPMQA YVGDLLAGKE GTRGKNFNMR
WIASMVADVH RILTRGGIFI YPWDKKDPSK AGKLRLMYEA NPMGLLVEQA GGAAWTGRER
ILDIQPDQLH QRVPVFLGSR EEVAEAVRYH HAHDNAQG
