ID Q5KQ48_CRYNJ Unreviewed; 350 AA. AC Q5KQ48; Q561E7; DT 15-FEB-2005, integrated into UniProtKB/TrEMBL. DT 15-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 112. DE RecName: Full=fructose-bisphosphatase {ECO:0000256|ARBA:ARBA00013093}; DE EC=3.1.3.11 {ECO:0000256|ARBA:ARBA00013093}; DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase {ECO:0000256|ARBA:ARBA00032973}; GN OrderedLocusNames=CNA00470 {ECO:0000313|EMBL:AAW40656.1}; OS Cryptococcus neoformans var. neoformans serotype D (strain JEC21 / ATCC OS MYA-565) (Filobasidiella neoformans). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes; OC Tremellales; Cryptococcaceae; Cryptococcus; OC Cryptococcus neoformans species complex. OX NCBI_TaxID=214684 {ECO:0000313|EMBL:AAW40656.1, ECO:0000313|Proteomes:UP000002149}; RN [1] {ECO:0000313|EMBL:AAW40656.1, ECO:0000313|Proteomes:UP000002149} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JEC21 / ATCC MYA-565 {ECO:0000313|Proteomes:UP000002149}; RX PubMed=15653466; DOI=10.1126/science.1103773; RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D., RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E., RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A., RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C., RA Janbon G., Jones S.J., Koo H.L., Krzywinski M.I., Kwon-Chung J.K., RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A., RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E., RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A., RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W., RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.; RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus RT neoformans."; RL Science 307:1321-1324(2005). CC -!- CATALYTIC ACTIVITY: CC Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6- CC phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; CC Evidence={ECO:0000256|ARBA:ARBA00001273}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000256|ARBA:ARBA00024331}. CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}. CC -!- SIMILARITY: Belongs to the FBPase class 1 family. CC {ECO:0000256|ARBA:ARBA00010941, ECO:0000256|RuleBase:RU000508}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE017341; AAW40656.1; -; Genomic_DNA. DR RefSeq; XP_566475.1; XM_566475.1. DR AlphaFoldDB; Q5KQ48; -. DR STRING; 214684.Q5KQ48; -. DR PaxDb; 214684-Q5KQ48; -. DR EnsemblFungi; AAW40656; AAW40656; CNA00470. DR GeneID; 3253502; -. DR KEGG; cne:CNA00470; -. DR VEuPathDB; FungiDB:CNA00470; -. DR eggNOG; KOG1458; Eukaryota. DR HOGENOM; CLU_039977_1_0_1; -. DR InParanoid; Q5KQ48; -. DR OMA; YIPENCP; -. DR OrthoDB; 292at2759; -. DR Proteomes; UP000002149; Chromosome 1. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0042597; C:periplasmic space; IEA:EnsemblFungi. DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0042149; P:cellular response to glucose starvation; IEA:EnsemblFungi. DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central. DR GO; GO:0006000; P:fructose metabolic process; IBA:GO_Central. DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central. DR GO; GO:0072593; P:reactive oxygen species metabolic process; IEA:EnsemblFungi. DR GO; GO:0005986; P:sucrose biosynthetic process; IBA:GO_Central. DR CDD; cd00354; FBPase; 1. DR Gene3D; 3.40.190.80; -; 1. DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1. DR HAMAP; MF_01855; FBPase_class1; 1. DR InterPro; IPR044015; FBPase_C_dom. DR InterPro; IPR000146; FBPase_class-1. DR InterPro; IPR033391; FBPase_N. DR InterPro; IPR028343; FBPtase. DR InterPro; IPR020548; Fructose_bisphosphatase_AS. DR PANTHER; PTHR11556; FRUCTOSE-1,6-BISPHOSPHATASE-RELATED; 1. DR PANTHER; PTHR11556:SF1; FRUCTOSE-BISPHOSPHATASE; 1. DR Pfam; PF00316; FBPase; 1. DR Pfam; PF18913; FBPase_C; 1. DR PIRSF; PIRSF500210; FBPtase; 1. DR PIRSF; PIRSF000904; FBPtase_SBPase; 1. DR PRINTS; PR00115; F16BPHPHTASE. DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1. DR PROSITE; PS00124; FBPASE; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, KW ECO:0000256|RuleBase:RU000508}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000508}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Reference proteome {ECO:0000313|Proteomes:UP000002149}. FT DOMAIN 20..208 FT /note="Fructose-1-6-bisphosphatase class I N-terminal" FT /evidence="ECO:0000259|Pfam:PF00316" FT DOMAIN 212..340 FT /note="Fructose-1-6-bisphosphatase class 1 C-terminal" FT /evidence="ECO:0000259|Pfam:PF18913" SQ SEQUENCE 350 AA; 37857 MW; 7DED8137041C786E CRC64; MAAPQATLGA DLEPPATDLI TLTRHILSQQ YALGESATGD LTMLLIAIQV TSKYIASNVR KARLINLVGL AGASNVQGED QKKLDVLSND IMVNALSASG KCSVMVSEEV DEAIIVSGIK GTYCVVFDPL DGSSNIDAGV NVGTIFGVYK VQEGSRGTVE DVLRPGREMV AAGYTMYGSS CNLVLSTGNG VDGFTLDESL GEFILTHPAI KIPSRGKIYS FNEGNSLHFY PPTNDYLNSI KYPENGKPYS ARYIGSMVAD VHRTLLYGGI FGYPDDKKSK DGKLRMLYEA FPMSFLTEQA GGVATTGSQR ILDIVPTSIH GRCPVFLGSK EDVEDLKKFY VNYKDDSRKW //