ID F16PA_HELPS Reviewed; 290 AA.
AC B2UVU9;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 01-MAY-2013, entry version 35.
DE RecName: Full=Fructose-1,6-bisphosphatase class 1;
DE Short=FBPase class 1;
DE EC=3.1.3.11;
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1;
GN Name=fbp; OrderedLocusNames=HPSH_07980;
OS Helicobacter pylori (strain Shi470).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=512562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shi470;
RA Kersulyte D., Kalia A., Gilman R.H., Berg D.E.;
RT "Genome sequence of Helicobacter pylori from the remote Amazon: traces
RT of Asian ancestry of the first Americans.";
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D-
CC fructose 6-phosphate + phosphate.
CC -!- COFACTOR: Binds 2 magnesium ions per subunit (By similarity).
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBUNIT: Homotetramer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (Potential).
CC -!- SIMILARITY: Belongs to the FBPase class 1 family.
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DR EMBL; CP001072; ACD48981.1; -; Genomic_DNA.
DR RefSeq; YP_001911011.1; NC_010698.2.
DR STRING; 512562.HPSH_07980; -.
DR EnsemblBacteria; ACD48981; ACD48981; HPSH_07980.
DR GeneID; 6296617; -.
DR KEGG; hps:HPSH_07980; -.
DR PATRIC; 20614529; VBIHelPyl23559_1550.
DR eggNOG; COG0158; -.
DR HOGENOM; HOG000191265; -.
DR KO; K03841; -.
DR OMA; HEKSECY; -.
DR ProtClustDB; PRK09293; -.
DR BioCyc; HPYL512562:GHHZ-1553-MONOMER; -.
DR UniPathway; UPA00138; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:HAMAP.
DR GO; GO:0000287; F:magnesium ion binding; IEA:HAMAP.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:HAMAP.
DR HAMAP; MF_01855; FBPase_class1; 1; -.
DR InterPro; IPR000146; FBPase_class-1/SBPase.
DR InterPro; IPR023079; SBPase.
DR PANTHER; PTHR11556; PTHR11556; 1.
DR Pfam; PF00316; FBPase; 1.
DR PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR PRINTS; PR01958; S17BPHPHTASE.
DR PROSITE; PS00124; FBPASE; FALSE_NEG.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Complete proteome; Cytoplasm; Hydrolase;
KW Magnesium; Metal-binding.
FT CHAIN 1 290 Fructose-1,6-bisphosphatase class 1.
FT /FTId=PRO_0000364576.
FT REGION 99 102 Substrate binding (By similarity).
FT METAL 78 78 Magnesium 1 (By similarity).
FT METAL 96 96 Magnesium 1 (By similarity).
FT METAL 96 96 Magnesium 2 (By similarity).
FT METAL 98 98 Magnesium 1; via carbonyl oxygen (By
FT similarity).
FT METAL 99 99 Magnesium 2 (By similarity).
FT METAL 232 232 Magnesium 2 (By similarity).
FT BINDING 201 201 Substrate (By similarity).
FT BINDING 226 226 Substrate (By similarity).
SQ SEQUENCE 290 AA; 32900 MW; F11EABD544AA3855 CRC64;
MDYKHFKGKH ANIVIEIISL LEKGVKKAQE ILEKPDAGSY TKLENSSGDT PIKADLALDK
FLEENFLSLE NVKSVFSEEK ETPVTKENGS YLIAYDPLDG SSVMEANFLV GTIIGVYEKD
YKAQNLAASL YVVFGHKIEL VVALEEVYRY GFYQNKFHFI ETIVLENKGK IIASGGNQKD
FSSGLKKALE GFFAENYRLR YSGSMVADVH HVLIKKGGMF SYPQKKLRKL FEVFPLALMV
EKAKGEAFYF DKGVKKRLLE QSVESYHEKS ECYLASQHEA HILEKYLKGE
//