DKFP_METJA
ID DKFP_METJA Reviewed; 310 AA.
AC Q58980;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Fructose-bisphosphate aldolase/6-deoxy-5-ketofructose 1-phosphate synthase;
DE EC=2.2.1.11 {ECO:0000269|PubMed:17014089};
DE EC=4.1.2.13 {ECO:0000269|PubMed:17014089};
DE AltName: Full=DKFP synthase;
DE AltName: Full=Fructose-bisphosphate aldolase class 1;
DE AltName: Full=Fructose-bisphosphate aldolase class I;
DE Short=FBP aldolase;
GN OrderedLocusNames=MJ1585;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION AS A FRUCTOSE-BISPHOSPHATE ALDOLASE AND DKFP SYNTHASE, AND
RP CATALYTIC ACTIVITY.
RX PubMed=17014089; DOI=10.1021/bi061018a;
RA White R.H., Xu H.;
RT "Methylglyoxal is an intermediate in the biosynthesis of 6-deoxy-5-
RT ketofructose-1-phosphate: a precursor for aromatic amino acid biosynthesis
RT in Methanocaldococcus jannaschii.";
RL Biochemistry 45:12366-12379(2006).
CC -!- FUNCTION: Catalyzes the transaldolization of either fructose-1-P or
CC fructose-1,6-bisphosphate with methylglyoxal to produce 6-deoxy-5-
CC ketofructose-1-phosphate (DKFP). Also catalyzes the reversible aldol
CC condensation of dihydroxyacetone phosphate (DHAP or glycerone-
CC phosphate) with glyceraldehyde 3-phosphate (G3P or GAP) to produce
CC fructose 1,6-bisphosphate (FBP). {ECO:0000269|PubMed:17014089}.
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:17014089};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate + methylglyoxal = 1-deoxy-D-
CC threo-hexo-2,5-diulose 6-phosphate + D-glyceraldehyde 3-phosphate;
CC Xref=Rhea:RHEA:31911, ChEBI:CHEBI:17158, ChEBI:CHEBI:32966,
CC ChEBI:CHEBI:58861, ChEBI:CHEBI:59776; EC=2.2.1.11;
CC Evidence={ECO:0000269|PubMed:17014089};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1-phosphate + methylglyoxal = 1-deoxy-D-threo-
CC hexo-2,5-diulose 6-phosphate + D-glyceraldehyde;
CC Xref=Rhea:RHEA:32259, ChEBI:CHEBI:17158, ChEBI:CHEBI:17378,
CC ChEBI:CHEBI:58861, ChEBI:CHEBI:138881; EC=2.2.1.11;
CC Evidence={ECO:0000269|PubMed:17014089};
CC -!- PATHWAY: Aromatic compound metabolism.
CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. {ECO:0000305}.
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DR EMBL; L77117; AAB99604.1; -; Genomic_DNA.
DR PIR; H64497; H64497.
DR AlphaFoldDB; Q58980; -.
DR SMR; Q58980; -.
DR STRING; 243232.MJ_1585; -.
DR EnsemblBacteria; AAB99604; AAB99604; MJ_1585.
DR KEGG; mja:MJ_1585; -.
DR eggNOG; arCOG04044; Archaea.
DR HOGENOM; CLU_057069_2_2_2; -.
DR InParanoid; Q58980; -.
DR OMA; FVKVNYP; -.
DR PhylomeDB; Q58980; -.
DR BioCyc; MetaCyc:MON-14590; -.
DR BRENDA; 2.2.1.11; 3260.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:UniProtKB.
DR GO; GO:0016744; F:transketolase or transaldolase activity; IDA:UniProtKB.
DR CDD; cd00958; DhnA; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR InterPro; IPR041720; FbaB-like.
DR Pfam; PF01791; DeoC; 1.
DR PIRSF; PIRSF038992; Aldolase_Ia; 1.
DR SMART; SM01133; DeoC; 1.
PE 1: Evidence at protein level;
KW Lyase; Reference proteome; Schiff base; Transferase.
FT CHAIN 1..310
FT /note="Fructose-bisphosphate aldolase/6-deoxy-5-
FT ketofructose 1-phosphate synthase"
FT /id="PRO_0000138958"
FT ACT_SITE 182
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 213
FT /note="Schiff-base intermediate with dihydroxyacetone-P"
FT /evidence="ECO:0000250"
FT ACT_SITE 213
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000250"
FT BINDING 48..49
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 213..215
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 241..243
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 270..271
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 310 AA; 34574 MW; 4AB6286F888049C0 CRC64;
MGIFMIKRLK KRDVKVPLTV PEDRKEEYIK NYLELTKRTG NVMLFAGDQK IEHLNDDFFG
EGIAKDDASP EHLFNIASKG KICGFATQLG LIARYGMDYK KIPYIVKINS KTHLVKTRDP
ISRALVHVKD VVDLKENSGL KILGVGYTIY PGSEYEHIMF EEASRVILEA HKHGLIAIIW
SYPRGKNVKD EKDPHLIAGA AGVAACLGAD FVKVNYPKCD NPAERFKEAV LAAGRTGVLC
AGGKSIEPEK FLKQIWEQIN ISGARGNATG RNIHQKPLDA AIRMCNAIYA ITIEGKSLEE
ALKIYYGDRK
