FUCA_METJA
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 03-AUG-2022, entry version 115.
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 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 OMA; ICRYGRS; -.
DR OrthoDB; 101802at2157; -.
DR PhylomeDB; Q58813; -.
DR BioCyc; MetaCyc:MON-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; -; 1.
DR InterPro; IPR001303; Aldolase_II/adducin_N.
DR InterPro; IPR036409; Aldolase_II/adducin_N_sf.
DR Pfam; PF00596; Aldolase_II; 1.
DR SMART; SM01007; Aldolase_II; 1.
DR SUPFAM; SSF53639; SSF53639; 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 wild-
FT 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
