FBPAP_PYRNV
ID FBPAP_PYRNV Reviewed; 399 AA.
AC B1YAL1;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Fructose-1,6-bisphosphate aldolase/phosphatase {ECO:0000303|PubMed:20348906, ECO:0000303|PubMed:21983965};
DE Short=FBP A/P {ECO:0000255|HAMAP-Rule:MF_02067};
DE Short=FBP aldolase/phosphatase {ECO:0000303|PubMed:20348906, ECO:0000303|PubMed:21983965};
DE EC=3.1.3.11 {ECO:0000269|PubMed:20348906, ECO:0000269|PubMed:21983965};
DE EC=4.1.2.13 {ECO:0000269|PubMed:20348906, ECO:0000269|PubMed:21983965};
GN Name=fbp {ECO:0000255|HAMAP-Rule:MF_02067};
GN OrderedLocusNames=Tneu_0133 {ECO:0000312|EMBL:ACB39090.1};
OS Pyrobaculum neutrophilum (strain DSM 2338 / JCM 9278 / NBRC 100436 /
OS V24Sta) (Thermoproteus neutrophilus).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=444157;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA Saltikov C., House C.H., Richardson P.;
RT "Complete sequence of Thermoproteus neutrophilus V24Sta.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION AS BOTH FBPASE AND FBP ALDOLASE, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=DSM 2338 / JCM 9278 / NBRC 100436 / V24Sta;
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] {ECO:0007744|PDB:3T2B, ECO:0007744|PDB:3T2C, ECO:0007744|PDB:3T2D, ECO:0007744|PDB:3T2E, ECO:0007744|PDB:3T2F, ECO:0007744|PDB:3T2G}
RP X-RAY CRYSTALLOGRAPHY (1.30 ANGSTROMS) OF WILD-TYPE AND MUTANT PHE-229 IN
RP COMPLEXES WITH MAGNESIUM; DHAP; FBP AND F6P, FUNCTION AS BOTH FBPASE AND
RP FBP ALDOLASE, CATALYTIC ACTIVITY, COFACTOR, DOMAIN, MUTAGENESIS OF TYR-229
RP AND ASP-297, REACTION MECHANISM, ACTIVE SITE, SCHIFF BASE FORMATION WITH
RP DHAP, AND SUBUNIT.
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, ECO:0000269|PubMed:21983965}.
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, ECO:0000269|PubMed:21983965};
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, ECO:0000269|PubMed:21983965};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21983965};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000305|PubMed:20348906}.
CC -!- SUBUNIT: Homooctamer; dimer of tetramers.
CC {ECO:0000269|PubMed:21983965}.
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:0000269|PubMed:21983965}.
CC -!- SIMILARITY: Belongs to the FBP aldolase/phosphatase family.
CC {ECO:0000255|HAMAP-Rule:MF_02067, ECO:0000305}.
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DR EMBL; CP001014; ACB39090.1; -; Genomic_DNA.
DR PDB; 3T2B; X-ray; 1.52 A; A=1-399.
DR PDB; 3T2C; X-ray; 1.30 A; A=1-399.
DR PDB; 3T2D; X-ray; 1.36 A; A=1-399.
DR PDB; 3T2E; X-ray; 1.66 A; A=1-399.
DR PDB; 3T2F; X-ray; 1.90 A; A=1-399.
DR PDB; 3T2G; X-ray; 3.00 A; A=1-399.
DR PDBsum; 3T2B; -.
DR PDBsum; 3T2C; -.
DR PDBsum; 3T2D; -.
DR PDBsum; 3T2E; -.
DR PDBsum; 3T2F; -.
DR PDBsum; 3T2G; -.
DR AlphaFoldDB; B1YAL1; -.
DR SMR; B1YAL1; -.
DR DIP; DIP-59163N; -.
DR STRING; 444157.Tneu_0133; -.
DR MoonProt; B1YAL1; -.
DR EnsemblBacteria; ACB39090; ACB39090; Tneu_0133.
DR KEGG; tne:Tneu_0133; -.
DR eggNOG; arCOG04180; Archaea.
DR HOGENOM; CLU_041630_0_0_2; -.
DR OMA; YMRRHGP; -.
DR BRENDA; 3.1.3.11; 6328.
DR BRENDA; 4.1.2.13; 6328.
DR UniPathway; UPA00138; -.
DR EvolutionaryTrace; B1YAL1; -.
DR Proteomes; UP000001694; 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 3D-structure; Carbohydrate metabolism; Gluconeogenesis; Hydrolase; Lyase;
KW Magnesium; Metal-binding; Schiff base.
FT CHAIN 1..399
FT /note="Fructose-1,6-bisphosphate aldolase/phosphatase"
FT /id="PRO_0000437183"
FT ACT_SITE 11
FT /note="Proton acceptor; for FBP phosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT ACT_SITE 229
FT /note="Proton donor/acceptor; for FBP aldolase activity"
FT /evidence="ECO:0000305|PubMed:21983965"
FT ACT_SITE 232
FT /note="Schiff-base intermediate with DHAP; for FBP aldolase
FT activity"
FT /evidence="ECO:0000269|PubMed:21983965"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21983965,
FT ECO:0007744|PDB:3T2B, ECO:0007744|PDB:3T2C,
FT ECO:0007744|PDB:3T2D"
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:0000269|PubMed:21983965,
FT ECO:0007744|PDB:3T2D"
FT BINDING 18
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000269|PubMed:21983965,
FT ECO:0007744|PDB:3T2C"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21983965,
FT ECO:0007744|PDB:3T2B, ECO:0007744|PDB:3T2C,
FT ECO:0007744|PDB:3T2D"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21983965,
FT ECO:0007744|PDB:3T2B, ECO:0007744|PDB:3T2C,
FT ECO:0007744|PDB:3T2D"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21983965,
FT ECO:0007744|PDB:3T2B, ECO:0007744|PDB:3T2C,
FT ECO:0007744|PDB:3T2D"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21983965,
FT ECO:0007744|PDB:3T2B, ECO:0007744|PDB:3T2C,
FT ECO:0007744|PDB:3T2D"
FT BINDING 91
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:0000269|PubMed:21983965,
FT ECO:0007744|PDB:3T2D"
FT BINDING 95
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21983965,
FT ECO:0007744|PDB:3T2C, ECO:0007744|PDB:3T2D,
FT ECO:0007744|PDB:3T2E"
FT BINDING 104..105
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:0000269|PubMed:21983965,
FT ECO:0007744|PDB:3T2D"
FT BINDING 132
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21983965,
FT ECO:0007744|PDB:3T2B, ECO:0007744|PDB:3T2C,
FT ECO:0007744|PDB:3T2D"
FT BINDING 133
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:0000269|PubMed:21983965,
FT ECO:0007744|PDB:3T2D"
FT BINDING 133
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000269|PubMed:21983965,
FT ECO:0007744|PDB:3T2C"
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 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:21983965"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000269|PubMed:21983965"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21983965,
FT ECO:0007744|PDB:3T2B, ECO:0007744|PDB:3T2C,
FT ECO:0007744|PDB:3T2D"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:21983965"
FT BINDING 242..243
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:0000269|PubMed:21983965"
FT BINDING 266
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:0000269|PubMed:21983965,
FT ECO:0007744|PDB:3T2D"
FT BINDING 266
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000269|PubMed:21983965,
FT ECO:0007744|PDB:3T2C"
FT BINDING 297
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:0000269|PubMed:21983965,
FT ECO:0007744|PDB:3T2D"
FT BINDING 297
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000269|PubMed:21983965,
FT ECO:0007744|PDB:3T2C"
FT BINDING 358
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:0000269|PubMed:21983965,
FT ECO:0007744|PDB:3T2D"
FT MUTAGEN 229
FT /note="Y->F: Shows unaltered FBP phosphatase activity,
FT whereas FBP aldolase activity is completely abolished."
FT /evidence="ECO:0000269|PubMed:21983965"
FT MUTAGEN 297
FT /note="D->N: 18-fold decrease in FBP phosphatase activity,
FT whereas FBP aldolase activity is completely abolished."
FT /evidence="ECO:0000269|PubMed:21983965"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:3T2C"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:3T2C"
FT HELIX 23..38
FT /evidence="ECO:0007829|PDB:3T2C"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:3T2C"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:3T2C"
FT HELIX 67..83
FT /evidence="ECO:0007829|PDB:3T2C"
FT TURN 84..89
FT /evidence="ECO:0007829|PDB:3T2C"
FT TURN 92..96
FT /evidence="ECO:0007829|PDB:3T2C"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:3T2E"
FT STRAND 102..105
FT /evidence="ECO:0007829|PDB:3T2D"
FT STRAND 112..119
FT /evidence="ECO:0007829|PDB:3T2C"
FT STRAND 122..134
FT /evidence="ECO:0007829|PDB:3T2C"
FT HELIX 136..139
FT /evidence="ECO:0007829|PDB:3T2C"
FT HELIX 140..148
FT /evidence="ECO:0007829|PDB:3T2C"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:3T2C"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:3T2C"
FT TURN 160..164
FT /evidence="ECO:0007829|PDB:3T2C"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:3T2C"
FT TURN 173..176
FT /evidence="ECO:0007829|PDB:3T2C"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:3T2C"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:3T2C"
FT HELIX 187..194
FT /evidence="ECO:0007829|PDB:3T2C"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:3T2C"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:3T2C"
FT TURN 208..210
FT /evidence="ECO:0007829|PDB:3T2C"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:3T2C"
FT HELIX 222..226
FT /evidence="ECO:0007829|PDB:3T2C"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:3T2D"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:3T2C"
FT STRAND 242..245
FT /evidence="ECO:0007829|PDB:3T2G"
FT HELIX 248..253
FT /evidence="ECO:0007829|PDB:3T2C"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:3T2C"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:3T2C"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:3T2C"
FT STRAND 279..282
FT /evidence="ECO:0007829|PDB:3T2C"
FT TURN 283..286
FT /evidence="ECO:0007829|PDB:3T2C"
FT STRAND 287..289
FT /evidence="ECO:0007829|PDB:3T2C"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:3T2C"
FT STRAND 301..310
FT /evidence="ECO:0007829|PDB:3T2C"
FT STRAND 313..319
FT /evidence="ECO:0007829|PDB:3T2C"
FT HELIX 324..341
FT /evidence="ECO:0007829|PDB:3T2C"
FT TURN 342..345
FT /evidence="ECO:0007829|PDB:3T2D"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:3T2C"
FT HELIX 353..356
FT /evidence="ECO:0007829|PDB:3T2C"
FT HELIX 361..366
FT /evidence="ECO:0007829|PDB:3T2C"
FT HELIX 373..388
FT /evidence="ECO:0007829|PDB:3T2C"
SQ SEQUENCE 399 AA; 44327 MW; 054A000B12A0453A CRC64;
MRVTVSIIKA DVGGFPGHAH VHPKMLEYAA AKLKEAQKRG VIIDYFVYNV GDDISLLMTH
TKGEDNKDIH GLAWETFKEV TDQIAKRFKL YGAGQDLLKD AFSGNIRGMG PQVAEMEFEE
RPSEPIIAFA ADKTEPGAFN LPLYKMFADP FTTAGLVIDP SMHEGFIFEV LDVVEHKVYL
LKTPEDAYSL LGLIGTTGRY IIRKVFRRAD GAPAAANSVE RLSLIAGRYV GKDDPVLLVR
AQSGLPAVGE VLEAFAHPHL VHGWMRGSHA GPLMPARFIS VDPERRIAIG PKMTRFDGPP
KVGALGFQLH EGYLEGGVDL FDDPAFDYVR QTAAQIADYI RRMGPFQPHR LPPEEMEYTA
LPKILAKVKP YPADQYEKDR KKYIEAVVKG AKVEESQHD
