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Database: UniProt
Entry: Q8U359_PYRFU
LinkDB: Q8U359_PYRFU
Original site: Q8U359_PYRFU 
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
//
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