ID   FUCA_METJA              Reviewed;         181 AA.
AC   Q58813;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 120.
DE   RecName: Full=L-fuculose phosphate aldolase {ECO:0000303|PubMed:16585745};
DE            EC=4.1.2.17 {ECO:0000269|PubMed:16585745, ECO:0000269|PubMed:17927915, ECO:0000269|PubMed:22418259, ECO:0000269|Ref.2};
DE   AltName: Full=L-fuculose-1-phosphate aldolase {ECO:0000303|PubMed:16585745};
GN   Name=fucA; OrderedLocusNames=MJ1418;
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, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
RP   ASN-25, AND COFACTOR.
RA   Yoon H.-S., Kwon S.-J., Han M.-S., Yu Y.-G., Yoon M.-Y.;
RT   "Mutagenic characterization of a conserved functional amino acid in
RT   fuculose-1-phosphate aldolase from Methanococcus jannaschii, a
RT   hyperthermophic archaea.";
RL   J. Microbiol. Biotechnol. 11:709-711(2001).
RN   [3]
RP   FUNCTION IN F420 BIOSYNTHESIS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, PATHWAY, AND SUBUNIT.
RX   PubMed=16585745; DOI=10.1128/jb.188.8.2836-2844.2006;
RA   Grochowski L.L., Xu H., White R.H.;
RT   "Identification of lactaldehyde dehydrogenase in Methanocaldococcus
RT   jannaschii and its involvement in production of lactate for F420
RT   biosynthesis.";
RL   J. Bacteriol. 188:2836-2844(2006).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX   PubMed=17927915; DOI=10.5483/bmbrep.2007.40.5.801;
RA   Nam Shin J.E., Kim M.J., Choi J.A., Chun K.H.;
RT   "Characterization of aldolase from Methanococcus jannaschii by gas
RT   chromatography.";
RL   J. Biochem. Mol. Biol. 40:801-804(2007).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY
RP   REGULATION.
RX   PubMed=22418259; DOI=10.1016/j.enzmictec.2012.01.001;
RA   Park H.C., Park J.S., Choi J.D., Dabrowski M., Atkins W.M., Yoon M.Y.;
RT   "Kinetic mechanism of fuculose-1-phosphate aldolase from the
RT   hyperthermophilic archaeon Methanococcus jannaschii.";
RL   Enzyme Microb. Technol. 50:209-214(2012).
CC   -!- FUNCTION: Involved in the biosynthesis of the coenzyme F420 which
CC       requires phospholactate produced via the aldol cleavage of L-fuculose
CC       1-phosphate and the NAD(+)-dependent oxidation of (S)-lactaldehyde
CC       (PubMed:16585745). Catalyzes the reversible cleavage of L-fuculose 1-
CC       phosphate (Fuc1P) to yield dihydroxyacetone phosphate (DHAP) and S-
CC       lactaldehyde (Ref.2, PubMed:16585745, PubMed:17927915,
CC       PubMed:22418259). FucA possesses a high specificity for the
CC       dihydroxyacetone phosphate (DHAP), but accepts a great variety of
CC       different aldehydes such as DL-glyceraldehyde and glycolaldehyde
CC       (PubMed:16585745, PubMed:17927915). {ECO:0000269|PubMed:16585745,
CC       ECO:0000269|PubMed:17927915, ECO:0000269|PubMed:22418259,
CC       ECO:0000269|Ref.2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-fuculose 1-phosphate = (S)-lactaldehyde + dihydroxyacetone
CC         phosphate; Xref=Rhea:RHEA:12933, ChEBI:CHEBI:18041,
CC         ChEBI:CHEBI:57642, ChEBI:CHEBI:57846; EC=4.1.2.17;
CC         Evidence={ECO:0000269|PubMed:16585745, ECO:0000269|PubMed:17927915,
CC         ECO:0000269|PubMed:22418259, ECO:0000269|Ref.2};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|Ref.2};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P0AB87};
CC   -!- ACTIVITY REGULATION: Trimethyl phosphonoacetate and DL-threose are
CC       competitive inhibitors with respect to dihydroxyacetone phosphate, and
CC       uncompetitive inhibitors with respect to DL-glyceraldehyde.
CC       {ECO:0000269|PubMed:22418259}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=90 uM for dihydroxyacetone phosphate (DHAP)
CC         {ECO:0000269|PubMed:22418259};
CC         KM=743 uM for DL-glyceraldehyde {ECO:0000269|PubMed:22418259};
CC         KM=7.8 mM for DL-glyceraldehyde (DHAP) {ECO:0000269|Ref.2};
CC         KM=1.01 mM for dihydroxyacetone phosphate (DHAP) {ECO:0000269|Ref.2};
CC         Vmax=0.0256 umol/min/mg enzyme (in the direction of aldol
CC         condensation) {ECO:0000269|PubMed:16585745};
CC         Vmax=0.0133 umol/min/mg enzyme (in the direction of hydrolysis)
CC         {ECO:0000269|PubMed:16585745};
CC         Vmax=570 nmol/min/mg enzyme with DL-lactaldehyde as substrate (at pH
CC         8 and at 70 degrees Celsius) {ECO:0000269|PubMed:16585745};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC       {ECO:0000305|PubMed:16585745}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16585745}.
CC   -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC       subfamily. {ECO:0000305}.
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DR   EMBL; L77117; AAB99428.1; -; Genomic_DNA.
DR   PIR; A64477; A64477.
DR   RefSeq; WP_010870936.1; NC_000909.1.
DR   AlphaFoldDB; Q58813; -.
DR   SMR; Q58813; -.
DR   STRING; 243232.MJ_1418; -.
DR   PaxDb; 243232-MJ_1418; -.
DR   EnsemblBacteria; AAB99428; AAB99428; MJ_1418.
DR   GeneID; 1452322; -.
DR   KEGG; mja:MJ_1418; -.
DR   eggNOG; arCOG04226; Archaea.
DR   HOGENOM; CLU_006033_3_1_2; -.
DR   InParanoid; Q58813; -.
DR   OrthoDB; 18709at2157; -.
DR   PhylomeDB; Q58813; -.
DR   BioCyc; MetaCyc:MONOMER-12176; -.
DR   BRENDA; 4.1.2.17; 3260.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IBA:GO_Central.
DR   GO; GO:0008738; F:L-fuculose-phosphate aldolase activity; IDA:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR   GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central.
DR   Gene3D; 3.40.225.10; Class II aldolase/adducin N-terminal domain; 1.
DR   InterPro; IPR001303; Aldolase_II/adducin_N.
DR   InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR   NCBIfam; NF040649; FucA_Meth; 1.
DR   PANTHER; PTHR22789:SF0; 3-OXO-TETRONATE 4-PHOSPHATE DECARBOXYLASE-RELATED; 1.
DR   PANTHER; PTHR22789; FUCULOSE PHOSPHATE ALDOLASE; 1.
DR   Pfam; PF00596; Aldolase_II; 1.
DR   SMART; SM01007; Aldolase_II; 1.
DR   SUPFAM; SSF53639; AraD/HMP-PK domain-like; 1.
PE   1: Evidence at protein level;
KW   Lyase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..181
FT                   /note="L-fuculose phosphate aldolase"
FT                   /id="PRO_0000162932"
FT   ACT_SITE        68
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         24..25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         39..40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         66..67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         147
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   MUTAGEN         25
FT                   /note="N->L: It shows a 3-fold increase of the affinty for
FT                   dihydroxyacetone phosphate (DHAP) and a 3-fold decrease of
FT                   the affinity for DL-glyceraldehyde compared to the
FT                   wild-type."
FT                   /evidence="ECO:0000269|Ref.2"
FT   MUTAGEN         25
FT                   /note="N->T: It shows a 5-fold decrease of the affinty for
FT                   dihydroxyacetone phosphate (DHAP), but has the same
FT                   affinity for DL-glyceraldehyde compared to the wild-type."
FT                   /evidence="ECO:0000269|Ref.2"
SQ   SEQUENCE   181 AA;  20470 MW;  E5F3BF13722145B0 CRC64;
     MDKKQFIKIC RKLYDRKYVV GSGGNVSVKE GDKIYLTPTG SILGFLKEDD IAEMDLDGNV
     IKGKPTSEKN LHLMIYRKRN DINAIIHTHS LISTFLSTIN KEIELLTPEG KIFLKKIGYV
     DYYEAGSLKL AEETAKRDED VIILKNHGVV CLGKDLIDAY IKVEVLEEQA KLTLLNLLVK
     K
//