ID   F16P_KLULA              Reviewed;         355 AA.
AC   Q05079;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 59.
DE   RecName: Full=Fructose-1,6-bisphosphatase;
DE            Short=FBPase;
DE            EC=3.1.3.11;
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase;
GN   Name=FBP1; OrderedLocusNames=KLLA0E01210g;
OS   Kluyveromyces lactis (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=28985;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SD11;
RX   MEDLINE=93185624; PubMed=8383039;
RX   DOI=10.1111/j.1432-1033.1993.tb17650.x;
RA   Zaror I., Marcus F., Moyer D.L., Tung J., Shuster J.R.;
RT   "Fructose-1,6-bisphosphatase of the yeast Kluyveromyces lactis.";
RL   Eur. J. Biochem. 212:193-199(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.-M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A.,
RA   Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D-
CC       fructose 6-phosphate + phosphate.
CC   -!- COFACTOR: Binds 3 magnesium ions per subunit (By similarity).
CC   -!- ENZYME REGULATION: Subject to complex allosteric regulation. The
CC       enzyme can assume an active R-state, or an inactive T-state.
CC       Intermediate conformations may exist. AMP acts as allosteric
CC       inhibitor. AMP binding affects the turnover of bound substrate and
CC       not the affinity for substrate (By similarity).
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SIMILARITY: Belongs to the FBPase class 1 family.
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DR   EMBL; X70181; CAA49728.1; -; Genomic_DNA.
DR   EMBL; CR382125; CAG99090.1; -; Genomic_DNA.
DR   PIR; S29397; S29397.
DR   RefSeq; XP_454003.1; -.
DR   HSSP; P00636; 1FBH.
DR   GeneID; 2894286; -.
DR   KEGG; kla:KLLA0E01210g; -.
DR   HOGENOM; Q05079; -.
DR   OMA; Q05079; MADQAPF.
DR   BRENDA; 3.1.3.11; 74088.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase act...; IEA:EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000146; Fructose_bisphosphatase.
DR   InterPro; IPR017955; IMPase/FBPase.
DR   PANTHER; PTHR11556; In_FB_phphtase; 1.
DR   Pfam; PF00316; FBPase; 1.
DR   PRINTS; PR00115; FBPHPHTASE.
DR   PRINTS; PR00377; INFBPHPHTASE.
DR   ProDom; PD001491; In_FB_phphtase; 1.
DR   PROSITE; PS00124; FBPASE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme; Carbohydrate metabolism; Complete proteome;
KW   Hydrolase; Magnesium; Metal-binding.
FT   INIT_MET      1      1       Removed (Probable).
FT   CHAIN         2    355       Fructose-1,6-bisphosphatase.
FT                                /FTId=PRO_0000200509.
FT   NP_BIND      37     41       AMP (By similarity).
FT   NP_BIND     121    122       AMP (By similarity).
FT   REGION      130    133       Substrate binding (By similarity).
FT   METAL        78     78       Magnesium 1 (By similarity).
FT   METAL       107    107       Magnesium 1 (By similarity).
FT   METAL       107    107       Magnesium 2 (By similarity).
FT   METAL       127    127       Magnesium 2 (By similarity).
FT   METAL       127    127       Magnesium 3 (By similarity).
FT   METAL       129    129       Magnesium 2; via carbonyl oxygen (By
FT                                similarity).
FT   METAL       130    130       Magnesium 3 (By similarity).
FT   METAL       300    300       Magnesium 3 (By similarity).
FT   BINDING     230    230       Substrate (By similarity).
FT   BINDING     264    264       Substrate (By similarity).
FT   BINDING     284    284       Substrate (By similarity).
FT   BINDING     294    294       Substrate (By similarity).
SQ   SEQUENCE   355 AA;  38899 MW;  3E24B69D32980AF6 CRC64;
     MAGIKHRRDS AESINTDIIT LSRFILDQQH LSAKNATGEF SMLLNSLQFA FKFISQTIRR
     AELVNLIGLA GASNSTGDQQ KKLDVLGDEI FINAMKASGN VKVLVSEEQE DLIVFRNSPG
     KYAVCCDPID GSSNLDAGVS VGTIVSLFKI HENQNGNSGE EDSEGTINDV ARCGREMVAA
     CYTMYGASTH LVLTTGAGVN GFTLDNNLGE FILTYPELRL PEQKSIYSIN EGNTCYWEPT
     IADFIAKLKE NSEENNGKPY SARYIGSMVA DVHRTLLYGG LFSYPGDKKN PNGKLRLLYE
     AFPMAFLVEQ AGGKAVNDRG ERILDLVPQH IHDKSSIWLG SSGDVDKYLK HIGKL
//