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Fructose-1,6-bisphosphate aldolase/phosphatase (FBP A/P) (FBP aldolase/phosphatase) (EC 3.1.3.11) (EC 4.1.2.13)

 B7R3I6_9EURY            Unreviewed;       375 AA.
B7R3I6;
10-FEB-2009, integrated into UniProtKB/TrEMBL.
10-FEB-2009, sequence version 1.
28-FEB-2018, entry version 30.
RecName: Full=Fructose-1,6-bisphosphate aldolase/phosphatase {ECO:0000256|HAMAP-Rule:MF_02067};
Short=FBP A/P {ECO:0000256|HAMAP-Rule:MF_02067};
Short=FBP aldolase/phosphatase {ECO:0000256|HAMAP-Rule:MF_02067};
EC=3.1.3.11 {ECO:0000256|HAMAP-Rule:MF_02067};
EC=4.1.2.13 {ECO:0000256|HAMAP-Rule:MF_02067};
Name=fbp {ECO:0000256|HAMAP-Rule:MF_02067};
ORFNames=TAM4_1210 {ECO:0000313|EMBL:EEB73462.1};
Thermococcus sp. AM4.
Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
Thermococcus.
NCBI_TaxID=246969 {ECO:0000313|EMBL:EEB73462.1, ECO:0000313|Proteomes:UP000009277};
[1] {ECO:0000313|EMBL:EEB73462.1, ECO:0000313|Proteomes:UP000009277}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AM4 {ECO:0000313|EMBL:EEB73462.1};
PubMed=22123768; DOI=10.1128/JB.06259-11;
Oger P., Sokolova T.G., Kozhevnikova D.A., Chernyh N.A.,
Bartlett D.H., Bonch-Osmolovskaya E.A., Lebedinsky A.V.;
"Complete Genome Sequence of the Hyperthermophilic Archaeon
Thermococcus sp. Strain AM4, Capable of Organotrophic Growth and
Growth at the Expense of Hydrogenogenic or Sulfidogenic Oxidation of
Carbon Monoxide.";
J. Bacteriol. 193:7019-7020(2011).
-!- FUNCTION: Catalyzes two subsequent steps in gluconeogenesis: the
aldol condensation of dihydroxyacetone phosphate (DHAP) and
glyceraldehyde-3-phosphate (GA3P) to fructose-1,6-bisphosphate
(FBP), and the dephosphorylation of FBP to fructose-6-phosphate
(F6P). {ECO:0000256|HAMAP-Rule:MF_02067}.
-!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D-
fructose 6-phosphate + phosphate. {ECO:0000256|HAMAP-
Rule:MF_02067}.
-!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone
phosphate + D-glyceraldehyde 3-phosphate. {ECO:0000256|HAMAP-
Rule:MF_02067}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_02067};
-!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
{ECO:0000256|HAMAP-Rule:MF_02067}.
-!- SUBUNIT: Homooctamer; dimer of tetramers. {ECO:0000256|HAMAP-
Rule:MF_02067}.
-!- DOMAIN: Consists of a single catalytic domain, but remodels its
active-site architecture via a large structural change to exhibit
dual activities. {ECO:0000256|HAMAP-Rule:MF_02067}.
-!- SIMILARITY: Belongs to the FBP aldolase/phosphatase family.
{ECO:0000256|HAMAP-Rule:MF_02067}.
-----------------------------------------------------------------------
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EMBL; CP002952; EEB73462.1; -; Genomic_DNA.
RefSeq; WP_014122810.1; NC_016051.1.
STRING; 246969.TAM4_1210; -.
EnsemblBacteria; EEB73462; EEB73462; TAM4_1210.
GeneID; 7420463; -.
KEGG; tha:TAM4_1210; -.
eggNOG; arCOG04180; Archaea.
eggNOG; COG1980; LUCA.
KO; K01622; -.
OrthoDB; POG093Z0396; -.
BioCyc; TSP246969:G1GNJ-1683-MONOMER; -.
UniPathway; UPA00138; -.
Proteomes; UP000009277; Chromosome.
GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-UniRule.
GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-UniRule.
GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniRule.
HAMAP; MF_02067; FBP_aldolase_phosphatase; 1.
InterPro; IPR002803; FBPase_V.
InterPro; IPR036076; FBPase_V_sf.
PANTHER; PTHR38341; PTHR38341; 1.
Pfam; PF01950; FBPase_3; 1.
PIRSF; PIRSF015647; FBPtase_archl; 1.
ProDom; PD014260; FBPase_V; 1.
SUPFAM; SSF111249; SSF111249; 1.
3: Inferred from homology;
Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_02067};
Complete proteome {ECO:0000313|Proteomes:UP000009277};
Gluconeogenesis {ECO:0000256|HAMAP-Rule:MF_02067};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_02067};
Lyase {ECO:0000256|HAMAP-Rule:MF_02067};
Magnesium {ECO:0000256|HAMAP-Rule:MF_02067};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_02067};
Schiff base {ECO:0000256|HAMAP-Rule:MF_02067}.
REGION 107 108 FBP binding. {ECO:0000256|HAMAP-
Rule:MF_02067}.
REGION 250 251 FBP binding; shared with dimeric partner.
{ECO:0000256|HAMAP-Rule:MF_02067}.
ACT_SITE 15 15 Proton acceptor; for FBP phosphatase
activity. {ECO:0000256|HAMAP-
Rule:MF_02067}.
ACT_SITE 237 237 Proton donor/acceptor; for FBP aldolase
activity. {ECO:0000256|HAMAP-
Rule:MF_02067}.
ACT_SITE 240 240 Schiff-base intermediate with DHAP; for
FBP aldolase activity.
{ECO:0000256|HAMAP-Rule:MF_02067}.
METAL 15 15 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_02067}.
METAL 22 22 Magnesium 1; via pros nitrogen.
{ECO:0000256|HAMAP-Rule:MF_02067}.
METAL 56 56 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_02067}.
METAL 56 56 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_02067}.
METAL 57 57 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_02067}.
METAL 98 98 Magnesium 1. {ECO:0000256|HAMAP-
Rule:MF_02067}.
METAL 135 135 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_02067}.
METAL 240 240 Magnesium 3; via carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_02067}.
METAL 241 241 Magnesium 3. {ECO:0000256|HAMAP-
Rule:MF_02067}.
METAL 241 241 Magnesium 4. {ECO:0000256|HAMAP-
Rule:MF_02067}.
METAL 242 242 Magnesium 2. {ECO:0000256|HAMAP-
Rule:MF_02067}.
METAL 242 242 Magnesium 3. {ECO:0000256|HAMAP-
Rule:MF_02067}.
BINDING 22 22 FBP; via tele nitrogen.
{ECO:0000256|HAMAP-Rule:MF_02067}.
BINDING 94 94 FBP. {ECO:0000256|HAMAP-Rule:MF_02067}.
BINDING 136 136 FBP/DHAP. {ECO:0000256|HAMAP-
Rule:MF_02067}.
BINDING 274 274 FBP/DHAP; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_02067}.
BINDING 295 295 FBP/DHAP. {ECO:0000256|HAMAP-
Rule:MF_02067}.
BINDING 357 357 FBP. {ECO:0000256|HAMAP-Rule:MF_02067}.
SEQUENCE 375 AA; 41837 MW; B346AAF62A9D7968 CRC64;
MAVGEKITIS VIKADIGGWP GHSRVHPQLI ETAEEILAKA KEEGTIIDFY VAYAGDDLQL
IMTHKKGVDS PDVHGLAWKA FEEATKVAKE LGLYGAGQDL LKDAFSGNVR GMGPGVAEME
ITLRKSEPIV TFHMDKTEPG AFNLPIFRMF ADPFNTAGLV IDPKMHMGFR FEVWDILKHK
RVILNTPEEV YDLLALIGAK SRYVIKRVYP KEGHPIPKDE PVAVVSTEKL YEIAGEYVGK
DDPVAIVRAQ SGLPALGEVL EPFAFPHLVS GWMRGSHNGP IMPVPMNYAN PTRFDGPPRV
VALGWQISPE GKLVGPVDLF DDPAYDYARQ KALEITEYMR RHGPFEPHRL PLEDMEYTTL
PGVLKRLEER FEDIE


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