(data stored in SCRATCH zone)

SWISSPROT: C5BF93_EDWI9

ID   C5BF93_EDWI9            Unreviewed;       334 AA.
AC   C5BF93;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 64.
DE   RecName: Full=Fructose-1,6-bisphosphatase class 1 {ECO:0000256|HAMAP-Rule:MF_01855};
DE            Short=FBPase class 1 {ECO:0000256|HAMAP-Rule:MF_01855};
DE            EC=3.1.3.11 {ECO:0000256|HAMAP-Rule:MF_01855};
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 {ECO:0000256|HAMAP-Rule:MF_01855};
GN   Name=fbp {ECO:0000256|HAMAP-Rule:MF_01855};
GN   OrderedLocusNames=NT01EI_0441 {ECO:0000313|EMBL:ACR67679.1};
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67679.1, ECO:0000313|Proteomes:UP000001485};
RN   [1] {ECO:0000313|Proteomes:UP000001485}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D-
CC       fructose 6-phosphate + phosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_01855, ECO:0000256|SAAS:SAAS00003077}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01855};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01855};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01855}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01855}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01855}.
CC   -!- SIMILARITY: Belongs to the FBPase class 1 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01855, ECO:0000256|RuleBase:RU000508,
CC       ECO:0000256|SAAS:SAAS00819920}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01855}.
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DR   EMBL; CP001600; ACR67679.1; -; Genomic_DNA.
DR   RefSeq; WP_015869882.1; NC_012779.2.
DR   ProteinModelPortal; C5BF93; -.
DR   STRING; 634503.NT01EI_0441; -.
DR   EnsemblBacteria; ACR67679; ACR67679; NT01EI_0441.
DR   GeneID; 7961266; -.
DR   KEGG; eic:NT01EI_0441; -.
DR   PATRIC; fig|634503.3.peg.401; -.
DR   eggNOG; ENOG4105CZI; Bacteria.
DR   eggNOG; COG0158; LUCA.
DR   HOGENOM; HOG000191265; -.
DR   KO; K03841; -.
DR   OMA; QSGLVCR; -.
DR   OrthoDB; POG091H05DB; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
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; C5BF93.
DR   SWISS-2DPAGE; C5BF93.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01855,
KW   ECO:0000256|RuleBase:RU000508, ECO:0000256|SAAS:SAAS00142634};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001485};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01855};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01855,
KW   ECO:0000256|RuleBase:RU000508, ECO:0000256|SAAS:SAAS00142646,
KW   ECO:0000313|EMBL:ACR67679.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01855};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01855};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001485}.
FT   DOMAIN        3    194       FBPase. {ECO:0000259|Pfam:PF00316}.
FT   REGION      115    118       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01855}.
FT   METAL        89     89       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
FT   METAL       112    112       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
FT   METAL       112    112       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
FT   METAL       114    114       Magnesium 1; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01855}.
FT   METAL       115    115       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
FT   METAL       277    277       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
FT   BINDING     208    208       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
FT   BINDING     241    241       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
FT   BINDING     271    271       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
SQ   SEQUENCE   334 AA;  37063 MW;  3047DD1FC13C7C75 CRC64;
     MKTLGEFIVE KQQDFPHATG ELTALLSAIK LGAKIIHRDI NKAGLVDIIG VSGAENIQGE
     VQMKLDLYAN EKLKAALEAR GEVAGIASEE EDDIVIFEGD RANNAKYVVL MDPLDGSSNI
     DVNVSVGTIF SIYRRITPLG TPVTREDFLQ PGNRQVAAGY VVYGSSTMLV YTTGNGVHAF
     TYDPSLGVFC LSHERLRFPH SSNMYSINEG NYIKFPLGVK KYIKYCQEQD SATQRPYTSR
     YIGSLVADFH RNLLKGGIYI YPSTASHPQG KLRLLYECNP MSFLAEQAGG KATDGFRRIL
     DIVPDQLHQR CPFFVGSCAM VEDAERFMHQ FPDE
//

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