ID   FUCA_METM5              Reviewed;         181 AA.
AC   A4FWY9;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=L-fuculose phosphate aldolase {ECO:0000250|UniProtKB:Q58813};
DE            EC=4.1.2.17 {ECO:0000250|UniProtKB:Q58813};
DE   AltName: Full=L-fuculose-1-phosphate aldolase {ECO:0000250|UniProtKB:Q58813};
GN   Name=fucA; OrderedLocusNames=MmarC5_0403;
OS   Methanococcus maripaludis (strain C5 / ATCC BAA-1333).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=402880;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C5 / ATCC BAA-1333;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C.,
RA   Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of chromosome of Methanococcus maripaludis C5.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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       Catalyzes the reversible cleavage of L-fuculose 1-phosphate (Fuc1P) to
CC       yield dihydroxyacetone phosphate (DHAP) and S-lactaldehyde.
CC       {ECO:0000250|UniProtKB:Q58813}.
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:0000250|UniProtKB:Q58813};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q58813};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P0AB87};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC       {ECO:0000250|UniProtKB:Q58813}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q58813}.
CC   -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC       subfamily. {ECO:0000250|UniProtKB:Q58813}.
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DR   EMBL; CP000609; ABO34718.1; -; Genomic_DNA.
DR   RefSeq; WP_011868173.1; NC_009135.1.
DR   AlphaFoldDB; A4FWY9; -.
DR   SMR; A4FWY9; -.
DR   STRING; 402880.MmarC5_0403; -.
DR   GeneID; 4928407; -.
DR   KEGG; mmq:MmarC5_0403; -.
DR   eggNOG; arCOG04226; Archaea.
DR   HOGENOM; CLU_006033_3_0_2; -.
DR   OrthoDB; 18709at2157; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000000253; Chromosome.
DR   GO; GO:0008738; F:L-fuculose-phosphate aldolase activity; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
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   3: Inferred from homology;
KW   Lyase; Metal-binding; Zinc.
FT   CHAIN           1..181
FT                   /note="L-fuculose phosphate aldolase"
FT                   /id="PRO_0000342595"
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"
SQ   SEQUENCE   181 AA;  20191 MW;  132B4FA5741F0DC7 CRC64;
     MNLSNFIKIC HLLYDRKYVV GSGGNVSIKN KNLIYITPTG SILGFLNEED ICVADIEGNI
     LKGKPTSELN MHLKIYQNKE SINAIVHTHS MYCTAFSALD KKLELLTPEA EIFIKKIAYV
     DYFPCGSLEL AENVSACVED SIILKNHGIV TLGKDITEAY VKTEVLEEIA QLNYIMNNLG
     E
//