F16PA_BRADU
ID F16PA_BRADU Reviewed; 345 AA.
AC Q8GKS1; Q79UB2;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=blr2581;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Fischer H.-M., Bauer E., Hennecke H.;
RT "The Bradyrhizobium japonicum cbb locus.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; AY150332; AAN61144.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC47846.1; -; Genomic_DNA.
DR RefSeq; NP_769221.1; NC_004463.1.
DR RefSeq; WP_011085367.1; NZ_CP011360.1.
DR AlphaFoldDB; Q8GKS1; -.
DR SMR; Q8GKS1; -.
DR STRING; 224911.27350837; -.
DR EnsemblBacteria; BAC47846; BAC47846; BAC47846.
DR GeneID; 64022332; -.
DR KEGG; bja:blr2581; -.
DR PATRIC; fig|224911.44.peg.2170; -.
DR eggNOG; COG0158; Bacteria.
DR HOGENOM; CLU_039977_0_0_5; -.
DR InParanoid; Q8GKS1; -.
DR OMA; HEKSECY; -.
DR PhylomeDB; Q8GKS1; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002526; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006000; P:fructose metabolic process; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0005986; P:sucrose biosynthetic process; IBA:GO_Central.
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 3: Inferred from homology;
KW Carbohydrate metabolism; Cytoplasm; Hydrolase; Magnesium; Metal-binding;
KW Reference proteome.
FT CHAIN 1..345
FT /note="Fructose-1,6-bisphosphatase class 1"
FT /id="PRO_0000364472"
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 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 111
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..115
FT /ligand="substrate"
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 200
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
FT BINDING 272
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01855"
SQ SEQUENCE 345 AA; 37113 MW; 4618B412FA7B5F0F CRC64;
MTGQLRLDDH LQRYSETAPH ALAVATAVDA IAAAAIEIAD LIGAGDLADA SGLTTGRNSD
GDVQRDLDVQ ADAILRRCLG KLSIAALASE EMREPQIGDR AARICVAIDP LDGSSNIDIN
MTVGTIFSIL PAPDDLALAF HQRGSAQFAA GFVTYGPQTS LVLTLGDGVD IFTLDRKAGC
FRLARSAIQI SEAGEEFAIN ASNRRHWDPP VRAFIDECLA GVEGPANHDF NMRWVGSLVA
EAYRILTRGG VFLYPSDARP GYGDGRLRLT YEAHPMAYII EQAGGSASTG RERILDLSAQ
SLHQRVPLIM GSSNEVRRVE ELHCDPLLVA SISAPLFARR GFFRL
