FBPAP_MOOTA
ID FBPAP_MOOTA Reviewed; 379 AA.
AC Q2RG86;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 84.
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=Moth_2266 {ECO:0000312|EMBL:ABC20553.1};
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
RN [2]
RP FUNCTION AS BOTH FBPASE AND FBP ALDOLASE, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC 39073 / JCM 9320;
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).
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:0000250|UniProtKB:F9VMT6};
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 remodels its active-
CC 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}.
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DR EMBL; CP000232; ABC20553.1; -; Genomic_DNA.
DR RefSeq; WP_011393749.1; NC_007644.1.
DR RefSeq; YP_431096.1; NC_007644.1.
DR AlphaFoldDB; Q2RG86; -.
DR SMR; Q2RG86; -.
DR STRING; 264732.Moth_2266; -.
DR EnsemblBacteria; ABC20553; ABC20553; Moth_2266.
DR KEGG; mta:Moth_2266; -.
DR PATRIC; fig|264732.11.peg.2469; -.
DR eggNOG; COG1980; Bacteria.
DR HOGENOM; CLU_041630_0_0_9; -.
DR OMA; YMRRHGP; -.
DR UniPathway; UPA00138; -.
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 1: Evidence at protein level;
KW Carbohydrate metabolism; Gluconeogenesis; Hydrolase; Lyase; Magnesium;
KW Metal-binding; Schiff base.
FT CHAIN 1..379
FT /note="Fructose-1,6-bisphosphate aldolase/phosphatase"
FT /id="PRO_0000437177"
FT ACT_SITE 13
FT /note="Proton acceptor; for FBP phosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT ACT_SITE 227
FT /note="Proton donor/acceptor; for FBP aldolase activity"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT ACT_SITE 230
FT /note="Schiff-base intermediate with DHAP; for FBP aldolase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 13
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 20
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 20
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 20
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 51
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 51
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
FT BINDING 130
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
FT BINDING 131
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
FT BINDING 264
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 285
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 285
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 346
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"
SQ SEQUENCE 379 AA; 42028 MW; 02F9E1B92FF5B844 CRC64;
MGERITLSVI KADIGGFVGH SSVHPRLLET AERYLAESKL LIDYRVAHVG DDIDLIMTHK
YGVDCPEIHH LAWNVFLQCT EVARELKLYG AGQDLLSDAF SGNVKGMGPG VAEMEFEERK
SEPIIVFAAD KTEPGAWNLP LYKMFADPFN TIGLVIDPKM HQGFRFEVYD LIKNERVEFS
LPEELYDLLV FIGAPGRYCI KSVYSKTTGE IAAVSSTQRL NLMAGRYVGK DDPVCIVRCQ
SGLPAVGEAL EPFANPHLVA GWMRGSHIGP LMPVGLDQSA PTRFDGPPRV VAMGFQLSGG
RLVGPQDFFG DVAFDKARQT ANEIASYLRS LGPFEPHRLP LEDMEYTTMP EVMAKLKNRF
VKVDHRDDRE PAAEELGAK
