ID F8C4Z5_THEGP Unreviewed; 368 AA.
AC F8C4Z5;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
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 OrderedLocusNames=TOPB45_0677 {ECO:0000313|EMBL:AEH22779.1};
OS Thermodesulfobacterium geofontis (strain OPF15).
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae;
OC Thermodesulfobacterium.
OX NCBI_TaxID=795359 {ECO:0000313|EMBL:AEH22779.1, ECO:0000313|Proteomes:UP000006583};
RN [1] {ECO:0000313|EMBL:AEH22779.1, ECO:0000313|Proteomes:UP000006583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OPF15 {ECO:0000313|EMBL:AEH22779.1,
RC ECO:0000313|Proteomes:UP000006583};
RX PubMed=23580711; DOI=10.1128/genomea.00162-13;
RA Elkins J.G., Hamilton-Brehm S.D., Lucas S., Han J., Lapidus A., Cheng J.F.,
RA Goodwin L.A., Pitluck S., Peters L., Mikhailova N., Davenport K.W.,
RA Detter J.C., Han C.S., Tapia R., Land M.L., Hauser L., Kyrpides N.C.,
RA Ivanova N.N., Pagani I., Bruce D., Woyke T., Cottingham R.W.;
RT "Complete genome sequence of the hyperthermophilic sulfate-reducing
RT bacterium Thermodesulfobacterium geofontis OPF15T.";
RL Genome Announc. 1:E0016213-E0016213(2013).
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}.
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; CP002829; AEH22779.1; -; Genomic_DNA.
DR RefSeq; WP_013909479.1; NC_015682.1.
DR AlphaFoldDB; F8C4Z5; -.
DR STRING; 795359.TOPB45_0677; -.
DR KEGG; top:TOPB45_0677; -.
DR PATRIC; fig|795359.3.peg.686; -.
DR eggNOG; COG1980; Bacteria.
DR HOGENOM; CLU_041630_0_0_0; -.
DR OrthoDB; 9763541at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000006583; 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};
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:UP000006583};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_02067}.
FT ACT_SITE 11
FT /note="Proton acceptor; for FBP phosphatase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT ACT_SITE 228
FT /note="Proton donor/acceptor; for FBP aldolase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT ACT_SITE 231
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 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 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 90
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 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 103..104
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 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 132
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 132
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 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="4"
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 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 265
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 265
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 286
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 286
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 347
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 368 AA; 40559 MW; 891AC821FE171761 CRC64;
MKLTLSVIKA DIGGFVGHSS VHKDVIEKVK EVAEDGKDKG IIRDVSILVC GDDIALVMTH
TKGVDSSEVH ELAWNAFKEG TEVAKKLKMY GAGQDLLADA FSGNIKGMGP GVAEMEFVER
KSEPVVIFFA DKTAPSAWNL PLYEIFADPM NTAGLVIDPS MHDGFIFDVM DVYTGMGIML
KAPEELYDLL VFIGATSRYV VRAVYRKSDG EIAASASTQR LSLMAGRYVG KDDPVLIVRA
QAGFPAVGEI LEPFARPWLV EGWMRGSHTG PLMPVSFKNA KPTRFDGPPR VIAAGYQITD
GYLIGPSDLF DDPAFDEARR QCNVMADILR RQGIFEPHRL PPEEMEYTTL PKVLEKLKDR
FKLVEAKK
//
