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   27-MAR-2024, entry version 104.
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   PaxDb; 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   PhylomeDB; Q58980; -.
DR   BioCyc; MetaCyc:MONOMER-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; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR002915; DeoC/FbaB/LacD_aldolase.
DR   InterPro; IPR041720; FbaB-like.
DR   PANTHER; PTHR47916; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 1; 1.
DR   PANTHER; PTHR47916:SF3; FRUCTOSE-BISPHOSPHATE ALDOLASE_6-DEOXY-5-KETOFRUCTOSE 1-PHOSPHATE SYNTHASE; 1.
DR   Pfam; PF01791; DeoC; 1.
DR   PIRSF; PIRSF038992; Aldolase_Ia; 1.
DR   SMART; SM01133; DeoC; 1.
DR   SUPFAM; SSF51569; Aldolase; 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
//