(data stored in ACNUC7421 zone)

SWISSPROT: F16PA_PSEPF

ID   F16PA_PSEPF             Reviewed;         336 AA.
AC   Q3KJG0;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 99.
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};
GN   OrderedLocusNames=Pfl01_0352;
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose
CC         6-phosphate + phosphate; Xref=Rhea:RHEA:11064,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57634; EC=3.1.3.11; Evidence={ECO:0000255|HAMAP-
CC         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.
CC       {ECO:0000255|HAMAP-Rule:MF_01855}.
DR   EMBL; CP000094; ABA72096.1; -; Genomic_DNA.
DR   RefSeq; WP_007952492.1; NC_007492.2.
DR   SMR; Q3KJG0; -.
DR   STRING; 205922.Pfl01_0352; -.
DR   PRIDE; Q3KJG0; -.
DR   EnsemblBacteria; ABA72096; ABA72096; Pfl01_0352.
DR   KEGG; pfo:Pfl01_0352; -.
DR   eggNOG; ENOG4105CZI; Bacteria.
DR   eggNOG; COG0158; LUCA.
DR   HOGENOM; HOG000191264; -.
DR   KO; K03841; -.
DR   OMA; QSGLVCR; -.
DR   BioCyc; PFLU205922:G1G4S-356-MONOMER; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000002704; 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; IPR000146; FBPase_class-1.
DR   InterPro; IPR033391; FBPase_N.
DR   InterPro; IPR028343; FBPtase.
DR   PANTHER; PTHR11556; PTHR11556; 1.
DR   Pfam; PF00316; FBPase; 1.
DR   PIRSF; PIRSF500210; FBPtase; 1.
DR   PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR   PRINTS; PR00115; F16BPHPHTASE.
PE   3: Inferred from homology;
DR   PRODOM; Q3KJG0.
DR   SWISS-2DPAGE; Q3KJG0.
KW   Carbohydrate metabolism; Complete proteome; Cytoplasm; Hydrolase;
KW   Magnesium; Metal-binding.
FT   CHAIN         1    336       Fructose-1,6-bisphosphatase class 1.
FT                                /FTId=PRO_0000364645.
FT   REGION      115    118       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   METAL        90     90       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   METAL       112    112       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   METAL       112    112       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   METAL       114    114       Magnesium 1; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01855}.
FT   METAL       115    115       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   METAL       283    283       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   BINDING     211    211       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   BINDING     277    277       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
SQ   SEQUENCE   336 AA;  37096 MW;  DAB979C39DFCB1E6 CRC64;
     MSRVTLSRYL IEQTRSNNTP ADLRFLIEVV ARACKEISHA VSKGALGGVL GSMGTENVQG
     EVQKKLDVLS NEILLEANEW GGHLAGMASE EMDNAYQIPG KYPKGAYLLV FDPLDGSSNI
     DINAPVGTIF SVLRCPNEYL SQNEALDEKA FLQPGTQQVA AGYAIYGPQT MLVLTLGHGV
     KGFTLDREMG SFVLTHEDIT IPESTQEFAI NMSNQRHWEA PVQRYVSELL AGEEGPLKKN
     YNMRWVAAMV ADVHRILTRG GLFMYPRDSR EPSKPGKLRL MYEANPMSFL VEQAGGASTD
     GHQRILDIKP EGLHQRVAVF LGSKEEVARA TAYHKE
//

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