(data stored in ACNUC7421 zone)

SWISSPROT: F16PA_STRM5

ID   F16PA_STRM5             Reviewed;         338 AA.
AC   B4SR24;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 67.
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=Smal_0020;
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001111; ACF49725.1; -; Genomic_DNA.
DR   RefSeq; WP_012509609.1; NC_011071.1.
DR   SMR; B4SR24; -.
DR   STRING; 391008.Smal_0020; -.
DR   PRIDE; B4SR24; -.
DR   EnsemblBacteria; ACF49725; ACF49725; Smal_0020.
DR   KEGG; smt:Smal_0020; -.
DR   eggNOG; ENOG4105CZI; Bacteria.
DR   eggNOG; COG0158; LUCA.
DR   HOGENOM; HOG000191264; -.
DR   KO; K03841; -.
DR   OMA; QSGLVCR; -.
DR   OrthoDB; 945770at2; -.
DR   BioCyc; SMAL391008:SMAL_RS00100-MONOMER; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001867; 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; B4SR24.
DR   SWISS-2DPAGE; B4SR24.
KW   Carbohydrate metabolism; Complete proteome; Cytoplasm; Hydrolase;
KW   Magnesium; Metal-binding.
FT   CHAIN         1    338       Fructose-1,6-bisphosphatase class 1.
FT                                /FTId=PRO_0000364724.
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       279    279       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   BINDING     207    207       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   BINDING     273    273       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
SQ   SEQUENCE   338 AA;  36796 MW;  9B489CE203E6FFEA CRC64;
     MSRTSLTRFL IQEQHAGRIN ADLRQLIAVV ARACTSISIA VSKGALGGVL GDAGTGNVQG
     EAQKKLDVIS NEILLEANAW GGHLAACASE EMDHSQPVPD IYPRGDFLLL FDPLDGSSNI
     DVNVSVGTIF SVLRCPTNVE LPGDDAFLQP GSKQIAAGYC IYGPSTQLVL TVGHGTHAFT
     LDREKGEFVL TTENMQIPAA TQEFAINMSN QRHWEAPMQA YVGDLLAGKE GARGKNFNMR
     WIASMVADVH RILTRGGIFI YPWDKKDPSK AGKLRLMYEA NPMGLLVEQA GGAAWTGRER
     ILDIQPDQLH QRVPVFLGSR EEVAEAVRYH HAHDDARG
//

If you have problems or comments...

PBIL Back to PBIL home page