ID   FUCA_METMP              Reviewed;         180 AA.
AC   Q6LY06;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 96.
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=MMP1187;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
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; BX950229; CAF30743.1; -; Genomic_DNA.
DR   RefSeq; WP_011171131.1; NC_005791.1.
DR   AlphaFoldDB; Q6LY06; -.
DR   SMR; Q6LY06; -.
DR   STRING; 267377.MMP1187; -.
DR   EnsemblBacteria; CAF30743; CAF30743; MMP1187.
DR   GeneID; 2762613; -.
DR   KEGG; mmp:MMP1187; -.
DR   PATRIC; fig|267377.15.peg.1220; -.
DR   eggNOG; arCOG04226; Archaea.
DR   HOGENOM; CLU_006033_3_4_2; -.
DR   OrthoDB; 18709at2157; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000000590; 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; Reference proteome; Zinc.
FT   CHAIN           1..180
FT                   /note="L-fuculose phosphate aldolase"
FT                   /id="PRO_0000342597"
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   180 AA;  20110 MW;  8EBD09B72341687D CRC64;
     MDLTEFIKIC RLLYDRKYVV GSGGNVSIRD GNLIYITPTG LSLGFLTKED ICIADLNGNI
     IKGKPTSELN MHLKIYQNKD SINAVVHTHS MYCTAFSALD KKLKLVTPEA EMVVKKIAYV
     DYFPCGSLEL AENVSECIED SIILKNHGIV TLGKDITEAY IKTEVLEEVA QLNYIMNNLK
//