FBPAP_CENSY
ID FBPAP_CENSY Reviewed; 376 AA.
AC A0RV30;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 2.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Fructose-1,6-bisphosphate aldolase/phosphatase {ECO:0000303|PubMed:20348906};
DE Short=FBP A/P {ECO:0000255|HAMAP-Rule:MF_02067};
DE Short=FBP aldolase/phosphatase {ECO:0000303|PubMed:20348906};
DE EC=3.1.3.11 {ECO:0000269|PubMed:20348906};
DE EC=4.1.2.13 {ECO:0000269|PubMed:20348906};
GN Name=fbp {ECO:0000255|HAMAP-Rule:MF_02067};
GN OrderedLocusNames=CENSYa_0564 {ECO:0000312|EMBL:ABK77197.1};
OS Cenarchaeum symbiosum (strain A).
OC Archaea; Thaumarchaeota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum.
OX NCBI_TaxID=414004;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A;
RX PubMed=17114289; DOI=10.1073/pnas.0608549103;
RA Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y.,
RA Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.;
RT "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum
RT symbiosum.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006).
RN [2]
RP FUNCTION AS BOTH FBPASE AND FBP ALDOLASE, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, MUTAGENESIS OF LYS-227 AND TYR-342,
RP ACTIVE SITE, AND SCHIFF BASE FORMATION WITH DHAP.
RC STRAIN=A;
RX PubMed=20348906; DOI=10.1038/nature08884;
RA Say R.F., Fuchs G.;
RT "Fructose 1,6-bisphosphate aldolase/phosphatase may be an ancestral
RT gluconeogenic enzyme.";
RL Nature 464:1077-1081(2010).
RN [3]
RP MUTAGENESIS OF TYR-224; LYS-227; ASP-228; GLU-341 AND TYR-342, AND ACTIVE
RP SITE.
RX PubMed=21983965; DOI=10.1038/nature10458;
RA Du J., Say R.F., Lu W., Fuchs G., Einsle O.;
RT "Active-site remodelling in the bifunctional fructose-1,6-bisphosphate
RT aldolase/phosphatase.";
RL Nature 478:534-537(2011).
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:0000269|PubMed:20348906}.
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:0000269|PubMed:20348906};
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:0000269|PubMed:20348906};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:20348906};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=40 uM for D-fructose 1,6-bisphosphate (when assaying the FBP
CC phosphatase activity, at 48 degrees Celsius)
CC {ECO:0000269|PubMed:20348906};
CC KM=110 uM for triosephosphates (when assaying the FBP aldolase
CC activity in the anabolic direction, at 48 degrees Celsius)
CC {ECO:0000269|PubMed:20348906};
CC KM=100 mM for D-fructose 1,6-bisphosphate (when assaying the FBP
CC aldolase activity in the catabolic direction, at 48 degrees Celsius)
CC {ECO:0000269|PubMed:20348906};
CC Vmax=0.22 umol/min/mg enzyme for the FBP phosphatase activity (at 48
CC degrees Celsius) {ECO:0000269|PubMed:20348906};
CC Vmax=0.24 umol/min/mg enzyme for the FBP aldolase activity in the
CC anabolic direction (at 48 degrees Celsius)
CC {ECO:0000269|PubMed:20348906};
CC Vmax=0.29 umol/min/mg enzyme for the FBP aldolase activity in the
CC catabolic direction (at 48 degrees Celsius)
CC {ECO:0000269|PubMed:20348906};
CC Note=The aldolase reaction is a classic case for a fully reversible
CC enzymatic reaction but here, the KM values for the substrate for the
CC aldol condensation and the aldol cleavage differ by a factor of 1000,
CC and the intrinsic phosphatase activity renders the process
CC irreversible. {ECO:0000269|PubMed:20348906};
CC Temperature dependence:
CC Heat-stabile at 70 degrees Celsius. Displays a half-life of 20
CC minutes at 82 degrees Celsius. {ECO:0000269|PubMed:20348906};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000305|PubMed:20348906}.
CC -!- SUBUNIT: Homooctamer; dimer of tetramers.
CC {ECO:0000250|UniProtKB:F9VMT6}.
CC -!- DOMAIN: Consists of a single catalytic domain, but remoldels its
CC active-site architecture via a large structural change to exhibit dual
CC activities. {ECO:0000250|UniProtKB:F9VMT6}.
CC -!- SIMILARITY: Belongs to the FBP aldolase/phosphatase family.
CC {ECO:0000255|HAMAP-Rule:MF_02067, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABK77197.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305|PubMed:20348906};
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DR EMBL; DP000238; ABK77197.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; A0RV30; -.
DR SMR; A0RV30; -.
DR STRING; 414004.CENSYa_0564; -.
DR EnsemblBacteria; ABK77197; ABK77197; CENSYa_0564.
DR KEGG; csy:CENSYa_0564; -.
DR PATRIC; fig|414004.10.peg.513; -.
DR HOGENOM; CLU_041630_0_0_2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000758; 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:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Gluconeogenesis; Hydrolase; Lyase; Magnesium;
KW Metal-binding; Oxidoreductase; Reference proteome; Schiff base.
FT CHAIN 1..376
FT /note="Fructose-1,6-bisphosphate aldolase/phosphatase"
FT /id="PRO_0000437179"
FT REGION 357..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 11
FT /note="Proton acceptor; for FBP phosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT ACT_SITE 224
FT /note="Proton donor/acceptor; for FBP aldolase activity"
FT /evidence="ECO:0000305|PubMed:21983965"
FT ACT_SITE 227
FT /note="Schiff-base intermediate with DHAP; for FBP aldolase
FT activity"
FT /evidence="ECO:0000269|PubMed:20348906"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
FT BINDING 18
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 87
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:0000250|UniProtKB:F9VMT6"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 100..101
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:0000250|UniProtKB:F9VMT6"
FT BINDING 128
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 129
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:0000250|UniProtKB:F9VMT6"
FT BINDING 129
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 227
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 229
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 237..238
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:0000250|UniProtKB:F9VMT6"
FT BINDING 261
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:0000250|UniProtKB:F9VMT6"
FT BINDING 261
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 342
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:0000250|UniProtKB:F9VMT6"
FT MUTAGEN 224
FT /note="Y->F: Shows slightly decreased FBP phosphatase
FT activity, whereas FBP aldolase activity is nearly
FT completely abolished."
FT /evidence="ECO:0000269|PubMed:21983965"
FT MUTAGEN 227
FT /note="K->R: Shows enhanced FBP phosphatase activity,
FT whereas FBP aldolase activity is completely abolished."
FT /evidence="ECO:0000269|PubMed:20348906,
FT ECO:0000269|PubMed:21983965"
FT MUTAGEN 228
FT /note="D->N: Shows completely abolition of both FBP
FT aldolase and FBP phosphatase activities."
FT /evidence="ECO:0000269|PubMed:21983965"
FT MUTAGEN 341
FT /note="E->Q: Shows unaltered FBP aldolase activity, whereas
FT FBP phosphatase activity is completely abolished."
FT /evidence="ECO:0000269|PubMed:21983965"
FT MUTAGEN 342
FT /note="Y->F: Shows unaltered FBP aldolase activity, whereas
FT FBP phosphatase activity is completely abolished."
FT /evidence="ECO:0000269|PubMed:20348906,
FT ECO:0000269|PubMed:21983965"
SQ SEQUENCE 376 AA; 41145 MW; E07465B9739B61E5 CRC64;
MRITVSAIKA DVGGIGGHTL PSSGLLDAVR RKVSSSSLLI DHYIGYCGDD VHIVMTHTRG
TDNSDIHKLA WDAFMEGTRV AKEEGLYGAG QDLLRDSFSG NVKGMGPGVA ELEFEERANE
AFTVFAADKT EPGAFNYPFY RMFVDSLSNT GLIVNKSLAE GVVINIMDVS KARTARLVLW
EDKPTIEAAL MYPGRFVVSS VETRDGEPIA SASTDRLHNI AGTYVGKDDP ICLVRTQKRF
PATEEAGSCF NNPHYVAGNT RGSHHMPLMP VRLNSPASIN FCIPIVEALV FSMHEGRLTG
PFDGFSTPDW DDVRRTATRR AHAMRRQGFV HPATLVPDEL EYAEGYRSRM DVLDSKMVPL
KDSGPAGTGR AYEDPD
