ID   FUCA_META3              Reviewed;         180 AA.
AC   A6UTG8;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 79.
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=Maeo_0198;
OS   Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS   Nankai-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=419665;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
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., Lykidis A.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus aeolicus Nankai-3.";
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; CP000743; ABR55790.1; -; Genomic_DNA.
DR   RefSeq; WP_011972922.1; NC_009635.1.
DR   AlphaFoldDB; A6UTG8; -.
DR   SMR; A6UTG8; -.
DR   STRING; 419665.Maeo_0198; -.
DR   GeneID; 75305571; -.
DR   KEGG; mae:Maeo_0198; -.
DR   eggNOG; arCOG04226; Archaea.
DR   HOGENOM; CLU_006033_3_4_2; -.
DR   OrthoDB; 18709at2157; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000001106; 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..180
FT                   /note="L-fuculose phosphate aldolase"
FT                   /id="PRO_0000342594"
FT   ACT_SITE        69
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         25..26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         40..41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         67..68
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         69
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P0AB87"
SQ   SEQUENCE   180 AA;  20464 MW;  2A0EAE2305C9839E CRC64;
     MDNLKEFIKI CHYLYDRKYV VGSGGNVSIK KDNLIYVTPT DSLLGFINEE DIAVVDMDGN
     IIKGAPTSEL YMHLNIYKKR NGVNAIVHTH SLYSTALPMA DKEIKLLTPE SRIFLKKIGY
     VDYFEARSME LANEVSKKDE DVIVLKNHGI VCVGKNLMDA YLKTEVMEEI SQLNYIIHSL
//