(data stored in ACNUC7421 zone)

SWISSPROT: F16A2_PARXL

ID   F16A2_PARXL             Reviewed;         378 AA.
AC   Q13QU8;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   07-JUN-2017, entry version 78.
DE   RecName: Full=Fructose-1,6-bisphosphatase class 1 2 {ECO:0000255|HAMAP-Rule:MF_01855};
DE            Short=FBPase class 1 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01855};
GN   Name=fbp2 {ECO:0000255|HAMAP-Rule:MF_01855};
GN   OrderedLocusNames=Bxeno_B0573; ORFNames=Bxe_B2450;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D-
CC       fructose 6-phosphate + phosphate. {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; CP000271; ABE33541.1; -; Genomic_DNA.
DR   RefSeq; WP_011490906.1; NZ_CP008762.1.
DR   ProteinModelPortal; Q13QU8; -.
DR   SMR; Q13QU8; -.
DR   STRING; 266265.Bxe_B2450; -.
DR   EnsemblBacteria; ABE33541; ABE33541; Bxe_B2450.
DR   GeneID; 4007054; -.
DR   KEGG; bxb:DR64_4778; -.
DR   KEGG; bxe:Bxe_B2450; -.
DR   PATRIC; fig|266265.5.peg.5259; -.
DR   eggNOG; ENOG4105CZI; Bacteria.
DR   eggNOG; COG0158; LUCA.
DR   HOGENOM; HOG000191264; -.
DR   KO; K03841; -.
DR   OMA; MSDRSPF; -.
DR   OrthoDB; POG091H05DB; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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   InterPro; IPR020548; Fructose_bisphosphatase_AS.
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.
DR   PROSITE; PS00124; FBPASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13QU8.
DR   SWISS-2DPAGE; Q13QU8.
KW   Carbohydrate metabolism; Complete proteome; Cytoplasm; Hydrolase;
KW   Magnesium; Metal-binding; Reference proteome.
FT   CHAIN         1    378       Fructose-1,6-bisphosphatase class 1 2.
FT                                /FTId=PRO_0000364507.
FT   REGION      123    126       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   METAL        98     98       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   METAL       120    120       Magnesium 1. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   METAL       120    120       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   METAL       122    122       Magnesium 1; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01855}.
FT   METAL       123    123       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   METAL       299    299       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   BINDING     227    227       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
SQ   SEQUENCE   378 AA;  41346 MW;  01910B54CF45B627 CRC64;
     MQDGRTTLSK FLIDTLDRQP CSTETARNAG LSALLIDVAA AIKSISAMLT KGALGGNYGS
     AQSINTHGEE QKKLDVATNE IFVQQCEWDG LLAAMVSEEM ESVYAIPPGY PRGDYLLAFD
     PLDGSSNIDI NGVVGSIFSV LRNGEGNGNA NEKNGSDPRG TVGESAFLRP GCEQVAAGYA
     VYGPSTMLVL SVGNGTHGFT LEREIGNFVL THSNIRIPED TVEFAINASN ERFWEPPVRR
     YVQECKDGRS GCRASDFNMR WIASMVAEVH RILMRGGVFM YPRDSKTPAM EGRLRLLYEA
     NPMSFLVEQA GGLSITGRER ILDVVPRALH GRVPVILGSK HEVERIGRYH GEYDRGEDQP
     FTSPLFSRRS LFLPGFTA
//

If you have problems or comments...

PBIL Back to PBIL home page