FBPAP_METTM
ID FBPAP_METTM Reviewed; 365 AA.
AC D9PUH5;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 51.
DE RecName: Full=Fructose-1,6-bisphosphate aldolase/phosphatase {ECO:0000303|PubMed:20348906};
DE Short=FBP A/P {ECO:0000255|HAMAP-Rule:MF_02067};
DE Short=FBP aldolase/phosphatase {ECO:0000303|PubMed:20348906};
DE EC=3.1.3.11 {ECO:0000269|PubMed:20348906};
DE EC=4.1.2.13 {ECO:0000269|PubMed:20348906};
GN Name=fbp {ECO:0000255|HAMAP-Rule:MF_02067};
GN OrderedLocusNames=MTBMA_c02650 {ECO:0000312|EMBL:ADL57873.1};
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
RN [2]
RP FUNCTION AS BOTH FBPASE AND FBP ALDOLASE, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
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).
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}.
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};
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};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:F9VMT6};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000305|PubMed:20348906}.
CC -!- SUBUNIT: Homooctamer; dimer of tetramers.
CC {ECO:0000250|UniProtKB:F9VMT6}.
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:0000250|UniProtKB:F9VMT6}.
CC -!- SIMILARITY: Belongs to the FBP aldolase/phosphatase family.
CC {ECO:0000255|HAMAP-Rule:MF_02067, ECO:0000305}.
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DR EMBL; CP001710; ADL57873.1; -; Genomic_DNA.
DR RefSeq; WP_013295100.1; NC_014408.1.
DR AlphaFoldDB; D9PUH5; -.
DR SMR; D9PUH5; -.
DR STRING; 79929.MTBMA_c02650; -.
DR EnsemblBacteria; ADL57873; ADL57873; MTBMA_c02650.
DR GeneID; 9703971; -.
DR KEGG; mmg:MTBMA_c02650; -.
DR PATRIC; fig|79929.8.peg.259; -.
DR HOGENOM; CLU_041630_0_0_2; -.
DR OMA; YMRRHGP; -.
DR OrthoDB; 21175at2157; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000345; 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..365
FT /note="Fructose-1,6-bisphosphate aldolase/phosphatase"
FT /id="PRO_0000437182"
FT ACT_SITE 11
FT /note="Proton acceptor; for FBP phosphatase activity"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT ACT_SITE 228
FT /note="Proton donor/acceptor; for FBP aldolase activity"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT ACT_SITE 231
FT /note="Schiff-base intermediate with DHAP; for FBP aldolase
FT activity"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 11
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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:0000250|UniProtKB:F9VMT6"
FT BINDING 18
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 18
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 53
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 90
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 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 103..104
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 131
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 132
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 132
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 231
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
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 232
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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:0000250|UniProtKB:F9VMT6"
FT BINDING 241..242
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:0000250|UniProtKB:F9VMT6"
FT BINDING 265
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 265
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 286
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 286
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250|UniProtKB:F9VMT6"
FT BINDING 347
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 365 AA; 40387 MW; 52268C30E96934C8 CRC64;
MKTTISVIKA DVGSVAGHAV AHEALKKKCD EILAEARDTG ILEDYYITNC GDDIDLIMTH
RNGEENEEVH QTAWNAFREA TEVARGLKLY GAGQDLLSDT FSGNIKGMGP GCAEMEFKER
PSDPVIIFCC DKTEPGAFNL PLFRMFADPF NTAGLVIDPT LHNGYEFEVF DVVEHKKVTM
ACPDEMYDLL ALLGSISRYV IKKIHRRDDG EIAASVSTER LNLMAGKYIG KDDPVAIVRA
QSGFPAAGEV VEPFAFPHLV GGWMRGSHNG PLMPVAQRDA TPVRFDGPPR VIGLGFQIAD
CKLVGPIDMF DDPSFDRSRQ LASEIAEYMR RHGPFEPHRL PSDEMEYTSL PGVLEKLGDR
FEDMD
