ID   FUCA_METVS              Reviewed;         181 AA.
AC   A6UPI8;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 71.
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=Mevan_0503;
OS   Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS   / SB).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
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; CP000742; ABR54410.1; -; Genomic_DNA.
DR   RefSeq; WP_011972313.1; NC_009634.1.
DR   AlphaFoldDB; A6UPI8; -.
DR   SMR; A6UPI8; -.
DR   STRING; 406327.Mevan_0503; -.
DR   EnsemblBacteria; ABR54410; ABR54410; Mevan_0503.
DR   GeneID; 5325627; -.
DR   KEGG; mvn:Mevan_0503; -.
DR   eggNOG; arCOG04226; Archaea.
DR   HOGENOM; CLU_006033_3_4_2; -.
DR   OMA; ICRYGRS; -.
DR   OrthoDB; 101802at2157; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000001107; 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; -; 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..181
FT                   /note="L-fuculose phosphate aldolase"
FT                   /id="PRO_0000342598"
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;  20301 MW;  2DCDB963BE47E88D CRC64;
     MDLKEFIKIC HLLYDRKYVV GSGGNVSLKK DNLVYITPTG SILGFLNEED ICVVDIAGKI
     IKGKPTSELN MHLEIYRNKP HVNAVVHTHS MYCTAFSVLD KKLELYTPEA EIFLKKIGYV
     DYCPCGTLEL AECVSSCNED VLILKKHGIV TLGSTLTEAY IKTEVLEEIA KLNHIVMSFD
     K