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Database: UniProt
Entry: A0A1D2WPW1_9EURY
LinkDB: A0A1D2WPW1_9EURY
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ID   A0A1D2WPW1_9EURY        Unreviewed;       193 AA.
AC   A0A1D2WPW1;
DT   30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   RecName: Full=L-fuculose phosphate aldolase {ECO:0000256|ARBA:ARBA00020613};
DE            EC=4.1.2.17 {ECO:0000256|ARBA:ARBA00013062};
DE   AltName: Full=L-fuculose-1-phosphate aldolase {ECO:0000256|ARBA:ARBA00030385};
GN   ORFNames=A9505_03465 {ECO:0000313|EMBL:OEC99920.1};
OS   Methanobrevibacter sp. A27.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX   NCBI_TaxID=1860099 {ECO:0000313|EMBL:OEC99920.1, ECO:0000313|Proteomes:UP000094786};
RN   [1] {ECO:0000313|EMBL:OEC99920.1, ECO:0000313|Proteomes:UP000094786}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A27 {ECO:0000313|EMBL:OEC99920.1,
RC   ECO:0000313|Proteomes:UP000094786};
RA   Woodcroft B.J.;
RT   "Validation of picogram- and femtogram-input DNA libraries for microscale
RT   metagenomics.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001277};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005036}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA
CC       subfamily. {ECO:0000256|ARBA:ARBA00010037}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OEC99920.1}.
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DR   EMBL; LZPL01000009; OEC99920.1; -; Genomic_DNA.
DR   RefSeq; WP_069573657.1; NZ_LZPL01000009.1.
DR   AlphaFoldDB; A0A1D2WPW1; -.
DR   UniPathway; UPA00071; -.
DR   Proteomes; UP000094786; Unassembled WGS sequence.
DR   GO; GO:0008738; F:L-fuculose-phosphate aldolase activity; IEA:UniProtKB-EC.
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   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;
FT   DOMAIN          6..183
FT                   /note="Class II aldolase/adducin N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01007"
SQ   SEQUENCE   193 AA;  21380 MW;  265198D2D4E4713E CRC64;
     MKKHINEIIN VSNEIYNKGL VSGKAGNISK RIKGSTGDIV AITPTLKSLS YLKEEDIVLV
     DMDGNLLTRG KPSSELNMHL EIYKKRSDVN AIVHTHSTYA TGFAFSSKKL KRLEGFGEIK
     NPYLNSIEYF KPGTSELAKN ASEGIKNEDV LILKNHGVIC VSDKLKEAKL LSIFVEESAK
     TQFVTCMLNS VED
//
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