ID   FUCA_METM7              Reviewed;         180 AA.
AC   A6VGC7;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=MmarC7_0434;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
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., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-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; CP000745; ABR65503.1; -; Genomic_DNA.
DR   RefSeq; WP_011976836.1; NC_009637.1.
DR   AlphaFoldDB; A6VGC7; -.
DR   SMR; A6VGC7; -.
DR   STRING; 426368.MmarC7_0434; -.
DR   EnsemblBacteria; ABR65503; ABR65503; MmarC7_0434.
DR   GeneID; 5328172; -.
DR   KEGG; mmz:MmarC7_0434; -.
DR   eggNOG; arCOG04226; Archaea.
DR   HOGENOM; CLU_006033_3_4_2; -.
DR   OMA; ICRYGRS; -.
DR   OrthoDB; 101802at2157; -.
DR   UniPathway; UPA00071; -.
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; -; 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   3: Inferred from homology;
KW   Lyase; Metal-binding; Zinc.
FT   CHAIN           1..180
FT                   /note="L-fuculose phosphate aldolase"
FT                   /id="PRO_0000342596"
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;  20039 MW;  D63FD14CF12562E1 CRC64;
     MDLINFIKIC HLLYDRKYVV GSGGNVSIRD GNHIYITPTG SILGFLNEED VCIVDLNGNI
     IKGKPTSELN MHLKIYQNKD CVNAIVHTHS MYCTAFSALD KKLELFTPEA EIVVKKIAYV
     DYSPCGSLEL AENVSSCVED SIILKNHGIV TVGKDITEAY VKTEVLEEIA QLNYIINNLK