(data stored in ACNUC9543 zone)

SWISSPROT: F16PA_YERPA

ID   F16PA_YERPA             Reviewed;         337 AA.
AC   Q1CBY3;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   08-MAY-2019, entry version 87.
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=YPA_0070;
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua;
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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; CP000308; ABG12039.1; -; Genomic_DNA.
DR   PIR; AI0427; AI0427.
DR   RefSeq; WP_002216946.1; NZ_CP009906.1.
DR   SMR; Q1CBY3; -.
DR   EnsemblBacteria; ABG12039; ABG12039; YPA_0070.
DR   KEGG; ypa:YPA_0070; -.
DR   HOGENOM; HOG000191265; -.
DR   KO; K03841; -.
DR   OMA; QSGLVCR; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001971; 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   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; Q1CBY3.
DR   SWISS-2DPAGE; Q1CBY3.
KW   Carbohydrate metabolism; Complete proteome; Cytoplasm; Hydrolase;
KW   Magnesium; Metal-binding.
FT   CHAIN         1    337       Fructose-1,6-bisphosphatase class 1.
FT                                /FTId=PRO_0000364762.
FT   REGION      115    118       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   METAL        89     89       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       277    277       Magnesium 2. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   BINDING     208    208       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   BINDING     241    241       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
FT   BINDING     271    271       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01855}.
SQ   SEQUENCE   337 AA;  36996 MW;  B6C41779F887FBA3 CRC64;
     MKTLGEFIVE KQLDFSHATG ELTALLSAIK LGAKIIHRDI NKAGLVDILG ASGVSNIQGE
     DQMKLDLFAN EKLKAALKAR GEVAGIASEE EDDIVIFDGG RAENAKYVVL MDPLDGSSNI
     DVNVSVGTIF SIYRRITPFG TPITEEDFLQ PGTKQVTAGY VVYGSSTMLV YTTGYGVHAF
     TYDPSLGVFC LSHEKVRYPA TGCMYSINEG NYIKFPLGVK KYIKYCQEQD EATKRPYTSR
     YIGSLVADFH RNLLKGGIYI YPSTASHPQG KLRLLYECNP MAFLAEQAGG KATDGVNRIL
     DIVPEKLHQR APFFVGTKSM VEDAEGFIAK FPDEEAK
//

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