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Database: UniProt
Entry: B2UVU9
LinkDB: B2UVU9
Original site: B2UVU9 
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
//
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