FBPAP_THEON
ID FBPAP_THEON Reviewed; 375 AA.
AC B6YTP6;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Fructose-1,6-bisphosphate aldolase/phosphatase {ECO:0000255|HAMAP-Rule:MF_02067};
DE Short=FBP A/P {ECO:0000255|HAMAP-Rule:MF_02067};
DE Short=FBP aldolase/phosphatase {ECO:0000255|HAMAP-Rule:MF_02067};
DE EC=3.1.3.11 {ECO:0000255|HAMAP-Rule:MF_02067, ECO:0000269|PubMed:21221938};
DE EC=4.1.2.13 {ECO:0000255|HAMAP-Rule:MF_02067};
GN Name=fbp {ECO:0000255|HAMAP-Rule:MF_02067};
GN OrderedLocusNames=TON_1497 {ECO:0000312|EMBL:ACJ16987.1};
OS Thermococcus onnurineus (strain NA1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1;
RX PubMed=18790866; DOI=10.1128/jb.00746-08;
RA Lee H.S., Kang S.G., Bae S.S., Lim J.K., Cho Y., Kim Y.J., Jeon J.H.,
RA Cha S.-S., Kwon K.K., Kim H.-T., Park C.-J., Lee H.-W., Kim S.I., Chun J.,
RA Colwell R.R., Kim S.-J., Lee J.-H.;
RT "The complete genome sequence of Thermococcus onnurineus NA1 reveals a
RT mixed heterotrophic and carboxydotrophic metabolism.";
RL J. Bacteriol. 190:7491-7499(2008).
RN [2]
RP FUNCTION AS A FBPASE, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=NA1;
RX PubMed=21221938; DOI=10.1007/s12275-010-0377-2;
RA Lee Y.G., Kang S.G., Lee J.H., Kim S.I., Chung Y.H.;
RT "Characterization of hyperthermostable fructose-1,6-bisphosphatase from
RT Thermococcus onnurineus NA1.";
RL J. Microbiol. 48:803-807(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) (By similarity).
CC Can also dephosphorylate, with lower activity, other related substrates
CC including fructose-1-phosphate, fructose-6-phosphate, glucose-1-
CC phosphate, glucose-6-phosphate, glycerol-2-phosphate,
CC phosphoenolpyruvate, 5'-AMP, 6'-ADP and 7'-ATP (PubMed:21221938).
CC {ECO:0000255|HAMAP-Rule:MF_02067, ECO:0000269|PubMed:21221938}.
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:0000255|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:0000255|HAMAP-Rule:MF_02067,
CC ECO:0000269|PubMed:21221938};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02067,
CC ECO:0000269|PubMed:21221938};
CC -!- ACTIVITY REGULATION: FBPase activity is inhibited by Ca(2+), ATP, ADP
CC and phosphoenolpyruvate. {ECO:0000269|PubMed:21221938}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.235 mM for FBP {ECO:0000269|PubMed:21221938};
CC Note=kcat is 14.84 sec(-1) for the FBPase activity (at 95 degrees
CC Celsius). {ECO:0000269|PubMed:21221938};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:21221938};
CC Temperature dependence:
CC Optimum temperature is 95 degrees Celsius.
CC {ECO:0000269|PubMed:21221938};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000255|HAMAP-Rule:MF_02067}.
CC -!- SUBUNIT: Homooctamer; dimer of tetramers. {ECO:0000255|HAMAP-
CC Rule:MF_02067, ECO:0000269|PubMed:21221938}.
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:0000255|HAMAP-Rule:MF_02067}.
CC -!- SIMILARITY: Belongs to the FBP aldolase/phosphatase family.
CC {ECO:0000255|HAMAP-Rule:MF_02067}.
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DR EMBL; CP000855; ACJ16987.1; -; Genomic_DNA.
DR RefSeq; WP_012572459.1; NC_011529.1.
DR AlphaFoldDB; B6YTP6; -.
DR SMR; B6YTP6; -.
DR STRING; 523850.TON_1497; -.
DR EnsemblBacteria; ACJ16987; ACJ16987; TON_1497.
DR GeneID; 7018533; -.
DR KEGG; ton:TON_1497; -.
DR PATRIC; fig|523850.10.peg.1509; -.
DR eggNOG; arCOG04180; Archaea.
DR HOGENOM; CLU_041630_0_0_2; -.
DR OMA; YMRRHGP; -.
DR OrthoDB; 21175at2157; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002727; 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 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..375
FT /note="Fructose-1,6-bisphosphate aldolase/phosphatase"
FT /id="PRO_0000442431"
FT ACT_SITE 15
FT /note="Proton acceptor; for FBP phosphatase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT ACT_SITE 237
FT /note="Proton donor/acceptor; for FBP aldolase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT ACT_SITE 240
FT /note="Schiff-base intermediate with DHAP; for FBP aldolase
FT activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT BINDING 15
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|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:0000250|UniProtKB:F9VMT6"
FT BINDING 22
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 22
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT BINDING 57
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|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:0000250|UniProtKB:F9VMT6"
FT BINDING 98
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_02067"
FT BINDING 135
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|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:0000250|UniProtKB:F9VMT6"
FT BINDING 136
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT BINDING 241
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02067"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|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:0000255|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:0000250|UniProtKB:F9VMT6"
FT BINDING 274
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
FT BINDING 295
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
SQ SEQUENCE 375 AA; 41875 MW; 83017926EB901A2B CRC64;
MAIGEKITIS VIKADIGGWP GHSRVHPQLI EAAEEVLAKA KEEGTIIDFY VAYAGDDLQL
IMTHKKGVDS PDIHGLAWKA FEEATEIAKE FGLYGAGQDL LKDAFSGNIR GMGPGIAEME
ITLRKSEPIV TFHMDKTEPG AFNLPIFRMF ADPFNTAGLV IDPNMHMGFR FEVWDIKEHK
RVILNTPEEI YDLLALIGAK SRYVIKRVYP KEGHKISKDE PVAVISTEKL YEIAGEYVGK
DDPVAIVRAQ SGLPALGEVL EPFAFPHLVS GWMRGSHNGP IMPVPMHQAN PTRFDGPPRV
VALGWQISPE GKLVGPVDLF DDPAFDYARQ KALEITEYIR RHGPFEPHRL PLEDMEYTTL
PGVLKKLEER FEDIE
