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FBPAP_METJA
ID   FBPAP_METJA             Reviewed;         389 AA.
AC   Q57747;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Fructose-1,6-bisphosphate aldolase/phosphatase {ECO:0000255|HAMAP-Rule:MF_02067};
DE            Short=FBP A/P {ECO:0000255|HAMAP-Rule:MF_02067};
DE            Short=FBP aldolase/phosphatase {ECO:0000255|HAMAP-Rule:MF_02067};
DE            EC=3.1.3.11 {ECO:0000255|HAMAP-Rule:MF_02067};
DE            EC=4.1.2.13 {ECO:0000255|HAMAP-Rule:MF_02067};
GN   Name=fbp {ECO:0000255|HAMAP-Rule:MF_02067}; OrderedLocusNames=MJ0299;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: Catalyzes two subsequent steps in gluconeogenesis: the aldol
CC       condensation of dihydroxyacetone phosphate (DHAP) and glyceraldehyde-3-
CC       phosphate (GA3P) to fructose-1,6-bisphosphate (FBP), and the
CC       dephosphorylation of FBP to fructose-6-phosphate (F6P).
CC       {ECO:0000255|HAMAP-Rule:MF_02067}.
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:0000255|HAMAP-Rule:MF_02067};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC         phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC         ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02067};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_02067};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000255|HAMAP-Rule:MF_02067}.
CC   -!- SUBUNIT: Homooctamer; dimer of tetramers. {ECO:0000255|HAMAP-
CC       Rule:MF_02067}.
CC   -!- DOMAIN: Consists of a single catalytic domain, but remodels its active-
CC       site architecture via a large structural change to exhibit dual
CC       activities. {ECO:0000255|HAMAP-Rule:MF_02067}.
CC   -!- SIMILARITY: Belongs to the FBP aldolase/phosphatase family.
CC       {ECO:0000255|HAMAP-Rule:MF_02067}.
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DR   EMBL; L77117; AAB98286.1; -; Genomic_DNA.
DR   PIR; D64337; D64337.
DR   AlphaFoldDB; Q57747; -.
DR   SMR; Q57747; -.
DR   STRING; 243232.MJ_0299; -.
DR   EnsemblBacteria; AAB98286; AAB98286; MJ_0299.
DR   KEGG; mja:MJ_0299; -.
DR   eggNOG; arCOG04180; Archaea.
DR   HOGENOM; CLU_041630_0_0_2; -.
DR   InParanoid; Q57747; -.
DR   OMA; YMRRHGP; -.
DR   PhylomeDB; Q57747; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_02067; FBP_aldolase_phosphatase; 1.
DR   InterPro; IPR002803; FBPase_V.
DR   InterPro; IPR036076; FBPase_V_sf.
DR   PANTHER; PTHR38341; PTHR38341; 1.
DR   Pfam; PF01950; FBPase_3; 1.
DR   PIRSF; PIRSF015647; FBPtase_archl; 1.
DR   SUPFAM; SSF111249; SSF111249; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Gluconeogenesis; Hydrolase; Lyase; Magnesium;
KW   Metal-binding; Reference proteome; Schiff base.
FT   CHAIN           1..389
FT                   /note="Fructose-1,6-bisphosphate aldolase/phosphatase"
FT                   /id="PRO_0000106782"
FT   ACT_SITE        17
FT                   /note="Proton acceptor; for FBP phosphatase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   ACT_SITE        233
FT                   /note="Proton donor/acceptor; for FBP aldolase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   ACT_SITE        236
FT                   /note="Schiff-base intermediate with DHAP; for FBP aldolase
FT                   activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         17
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         24
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         24
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         24
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         57
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         57
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         58
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         95
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         99
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         108..109
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         136
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         137
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         137
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         236
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         238
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         238
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         246..247
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         270
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         270
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         291
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         291
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT   BINDING         352
FT                   /ligand="beta-D-fructose 1,6-bisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:32966"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
SQ   SEQUENCE   389 AA;  43246 MW;  1BB8D890F931CE73 CRC64;
     MSRMENNKVT ISVIKADVGG LCGHTLAPDE LLEACEAVLE EAVDEIILDY YVTRCGDDID
     LIMSHKLGCD NEKVHGLAWR AFEEATKVAK ELKLYGAGQD LLADSFSGNV RGMGPGCAEM
     EFVERKSEPI VVFCCDKTDP TAFNYPLFKM FADPFNTAGL VFDPSMISGF KFEVHDVVGH
     KKVFLDTPEE MYMLLALIGD YEKYAIKRVY RRRDNEIAAV VSTEKLNYIA GEYVGKDDPV
     AIVRAQSGFP AVGEVLEPFA NPHFVPGWMR GSHWGPLMPV GEEDATPTRF DGPARIIALG
     FQVCDGMLIG PNDLFADKGF DKAREKALEM ADIIRRMGPF QPHRLPATMM EYTTVPKVLE
     ALEDRFIPLE GLELIEEGGI TRKDRGDVE
 
 
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