ID K0I7L4_NITGG Unreviewed; 385 AA.
AC K0I7L4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Fructose-1,6-bisphosphate aldolase/phosphatase {ECO:0000256|ARBA:ARBA00018635, ECO:0000256|HAMAP-Rule:MF_02067};
DE Short=FBP A/P {ECO:0000256|HAMAP-Rule:MF_02067};
DE Short=FBP aldolase/phosphatase {ECO:0000256|HAMAP-Rule:MF_02067};
DE EC=3.1.3.11 {ECO:0000256|ARBA:ARBA00013093, ECO:0000256|HAMAP-Rule:MF_02067};
DE EC=4.1.2.13 {ECO:0000256|HAMAP-Rule:MF_02067};
GN Name=fbp {ECO:0000256|HAMAP-Rule:MF_02067,
GN ECO:0000313|EMBL:AFU57241.1};
GN OrderedLocusNames=Ngar_c02930 {ECO:0000313|EMBL:AFU57241.1};
OS Nitrososphaera gargensis (strain Ga9.2).
OC Archaea; Nitrososphaerota; Nitrososphaeria; Nitrososphaerales;
OC Nitrososphaeraceae; Nitrososphaera.
OX NCBI_TaxID=1237085 {ECO:0000313|EMBL:AFU57241.1, ECO:0000313|Proteomes:UP000008037};
RN [1] {ECO:0000313|EMBL:AFU57241.1, ECO:0000313|Proteomes:UP000008037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ga9.2 {ECO:0000313|Proteomes:UP000008037};
RX PubMed=23057602; DOI=10.1111/j.1462-2920.2012.02893.x;
RA Spang A., Poehlein A., Offre P., Zumbragel S., Haider S., Rychlik N.,
RA Nowka B., Schmeisser C., Lebedeva E.V., Rattei T., Bohm C., Schmid M.,
RA Galushko A., Hatzenpichler R., Weinmaier T., Daniel R., Schleper C.,
RA Spieck E., Streit W., Wagner M.;
RT "The genome of the ammonia-oxidizing Candidatus Nitrososphaera gargensis:
RT insights into metabolic versatility and environmental adaptations.";
RL Environ. Microbiol. 14:3122-45(2012).
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:0000256|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:0000256|ARBA:ARBA00001273, ECO:0000256|HAMAP-
CC 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:0000256|HAMAP-Rule:MF_02067};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_02067};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742, ECO:0000256|HAMAP-Rule:MF_02067}.
CC -!- SUBUNIT: Homooctamer; dimer of tetramers.
CC {ECO:0000256|ARBA:ARBA00011820, ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_02067}.
CC -!- SIMILARITY: Belongs to the FBP aldolase/phosphatase family.
CC {ECO:0000256|ARBA:ARBA00010693, ECO:0000256|HAMAP-Rule:MF_02067}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02067}.
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DR EMBL; CP002408; AFU57241.1; -; Genomic_DNA.
DR AlphaFoldDB; K0I7L4; -.
DR STRING; 1237085.Ngar_c02930; -.
DR KEGG; nga:Ngar_c02930; -.
DR PATRIC; fig|1237085.11.peg.286; -.
DR HOGENOM; CLU_041630_0_0_2; -.
DR InParanoid; K0I7L4; -.
DR OrthoDB; 5829at2157; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000008037; 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 NCBIfam; NF041126; FBP_aldo_phos; 1.
DR PANTHER; PTHR38341; FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE/PHOSPHATASE; 1.
DR PANTHER; PTHR38341:SF1; FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE_PHOSPHATASE; 1.
DR Pfam; PF01950; FBPase_3; 1.
DR PIRSF; PIRSF015647; FBPtase_archl; 1.
DR SUPFAM; SSF111249; Sulfolobus fructose-1,6-bisphosphatase-like; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_02067}; Coiled coil {ECO:0000256|SAM:Coils};
KW Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432, ECO:0000256|HAMAP-
KW Rule:MF_02067};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_02067};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02067};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_02067};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_02067}; Reference proteome {ECO:0000313|Proteomes:UP000008037};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_02067}.
FT COILED 346..373
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 11
FT /note="Proton acceptor; for FBP phosphatase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT ACT_SITE 227
FT /note="Proton donor/acceptor; for FBP aldolase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT ACT_SITE 230
FT /note="Schiff-base intermediate with DHAP; for FBP aldolase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 18
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 18
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:0000256|HAMAP-Rule:MF_02067"
FT BINDING 51
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 51
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 89
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:0000256|HAMAP-Rule:MF_02067"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 102..103
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:0000256|HAMAP-Rule:MF_02067"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 131
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 131
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:0000256|HAMAP-Rule:MF_02067"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 240..241
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:0000256|HAMAP-Rule:MF_02067"
FT BINDING 264
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 264
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:0000256|HAMAP-Rule:MF_02067"
FT BINDING 345
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:0000256|HAMAP-Rule:MF_02067"
SQ SEQUENCE 385 AA; 42383 MW; C0B3B460A834E107 CRC64;
MQITVSAIKA DIGGIGGHTR PSDELLETVR NFVAKNSKGL LIDHYIGYTG DDIHIIMTHT
RGVDDEKIHK LAWDAFTEGT KTAKEQGLYG AGQDLLKDSF SGNVKGMGPG VAEIEMEERP
SEVFCIFAAD KTEPGAFNFP LWRMFVDARS NSGLLINERL AEGVVFRIMD VMTGKVAELK
MWQDKAELEA ALMYPGRYVV HSVVSADGTD QIVSASTDRL HNIAGTYVGK DDPIAIVRTQ
KNFPATEEAG SAFNDPHYVA GNTRGSHHMP LMPVKLNSAA SLNYSIPIVS CLLFSMHNGK
LTGPHDGFGT ADWDLQRMWA AERAMIMRNQ GFIHPATLVP DELEYNKGYE ARMSKLESKF
RNLEDIMNGK TKKAATKAKE AGSKR
//
