ID Q8U359_PYRFU Unreviewed; 375 AA.
AC Q8U359;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 24-JAN-2024, entry version 89.
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=PF0613 {ECO:0000313|EMBL:AAL80737.1};
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497 {ECO:0000313|EMBL:AAL80737.1, ECO:0000313|Proteomes:UP000001013};
RN [1] {ECO:0000313|EMBL:AAL80737.1, ECO:0000313|Proteomes:UP000001013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1
RC {ECO:0000313|Proteomes:UP000001013};
RX PubMed=10430560;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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}.
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DR EMBL; AE009950; AAL80737.1; -; Genomic_DNA.
DR RefSeq; WP_011011733.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U359; -.
DR STRING; 186497.PF0613; -.
DR PaxDb; 186497-PF0613; -.
DR GeneID; 41712418; -.
DR KEGG; pfu:PF0613; -.
DR PATRIC; fig|186497.12.peg.644; -.
DR eggNOG; arCOG04180; Archaea.
DR HOGENOM; CLU_041630_0_0_2; -.
DR OMA; YMRRHGP; -.
DR OrthoDB; 5829at2157; -.
DR PhylomeDB; Q8U359; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001013; 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:UP000001013};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_02067}.
FT ACT_SITE 15
FT /note="Proton acceptor; for FBP phosphatase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT ACT_SITE 237
FT /note="Proton donor/acceptor; for FBP aldolase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT ACT_SITE 240
FT /note="Schiff-base intermediate with DHAP; for FBP aldolase
FT activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 22
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 22
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 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 57
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 94
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 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 107..108
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 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 136
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 136
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 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 250..251
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 274
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 274
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 295
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT BINDING 295
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 357
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 375 AA; 41827 MW; 39E0AB14FE63345A CRC64;
MAVGEKITIS VIKADVGGWP GHSRVHPALI ERAKEVLSEA QKEGTLIDFY VTYAGDDLQL
IMTHKKGVDS PEIHGLAWEA FKKATEVAKE LGLYGAGQDL LKDAFSGNVR GLGPSVAEME
ITLRKSEPIV TFHLDKTEPG AFNLPIFRMF ADPFNTAGLV IDPKMHMGFR FEIWDILEHK
RVIMNSPEEM YDILALIGAK SRYVIKRVYP KEGHPIPKDE PVAVVSTEKL YEVAGEYVGK
DDPVAIVRAQ SGLPALGEVL EPFAFPHLVS GWMRGSHNGP LMPVPLKYAT PTRFDGPPRA
VALGWQISPE GKLIGPVDLF DDPAFDWARQ KALEITDYMR RHGPFEPHRL PLEEMEYTTL
PGVLEKLKDR FEPIE
//