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Database: UniProt
Entry: A0A0M0BC59_9ARCH
LinkDB: A0A0M0BC59_9ARCH
Original site: A0A0M0BC59_9ARCH 
ID   A0A0M0BC59_9ARCH        Unreviewed;       372 AA.
AC   A0A0M0BC59;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
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   ORFNames=AC480_06350 {ECO:0000313|EMBL:KON26128.1};
OS   miscellaneous Crenarchaeota group archaeon SMTZ1-55.
OC   Archaea; Candidatus Bathyarchaeota.
OX   NCBI_TaxID=1685133 {ECO:0000313|EMBL:KON26128.1, ECO:0000313|Proteomes:UP000037456};
RN   [1] {ECO:0000313|EMBL:KON26128.1, ECO:0000313|Proteomes:UP000037456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMTZ1-55 {ECO:0000313|EMBL:KON26128.1};
RA   Lazar C.S., Baker B.J., Seitz K.W., Hyde A.S., Dick G.J., Hinrichs K.-U.,
RA   Teske A.P.;
RT   "New insights into the roles of widespread benthic archaea in carbon and
RT   nitrogen cycling.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KON26128.1}.
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DR   EMBL; LFWX01000126; KON26128.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M0BC59; -.
DR   PATRIC; fig|1685133.3.peg.1507; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000037456; Unassembled WGS sequence.
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};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW   Rule:MF_02067}.
FT   ACT_SITE        12
FT                   /note="Proton acceptor; for FBP phosphatase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT   ACT_SITE        229
FT                   /note="Proton donor/acceptor; for FBP aldolase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT   ACT_SITE        232
FT                   /note="Schiff-base intermediate with DHAP; for FBP aldolase
FT                   activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT   BINDING         12
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT   BINDING         19
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT   BINDING         19
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT   BINDING         19
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         53
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT   BINDING         53
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT   BINDING         54
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
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:0000256|HAMAP-Rule:MF_02067"
FT   BINDING         95
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
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:0000256|HAMAP-Rule:MF_02067"
FT   BINDING         132
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT   BINDING         133
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
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:0000256|HAMAP-Rule:MF_02067"
FT   BINDING         232
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT   BINDING         233
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="4"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT   BINDING         233
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT   BINDING         234
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT   BINDING         234
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..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:0000256|HAMAP-Rule:MF_02067"
FT   BINDING         266
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
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:0000256|HAMAP-Rule:MF_02067"
FT   BINDING         287
FT                   /ligand="dihydroxyacetone phosphate"
FT                   /ligand_id="ChEBI:CHEBI:57642"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02067"
FT   BINDING         287
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         355
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   372 AA;  40653 MW;  D5E4936242F8471A CRC64;
     MVKTTVSLIK ADVGSLAGHT VVPEPLLKVA RERMEEAKES DVINSYYVFN AGDDLELLMT
     HGRGVNSEEV HGLAWNTFNA AADKAKKLKL YGAGQDLLVD AFSGNVRGMG PGVAEMEFEE
     RRSDPMIVYA ADKTEPAAYN YLLYKIFADP FNTAGLVIDP RMVSGYKFEV LDAIESKTVV
     LKTPEEAYSL LALIGTTERY MISRILRASD DEIAASSSTT KLALIAGKYV GKDDPVCLVR
     GQSGFPAMGE ITAPLLHTYL VAGWMRGSHW GPFMPVGLKD SRCTVFDGPP RIVALGVQIA
     DGRLVSDDEG NPLIADIFAD PAFDMARREA LELASHLRRM GEFEPARLGP GAMEYTTLPQ
     VLKQLEPRFK KA
//
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