ID U6EEX2_9EURY Unreviewed; 192 AA.
AC U6EEX2;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=MBMB1_2028 {ECO:0000313|EMBL:CDG66102.1};
OS Methanobacterium sp. MB1.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobacterium.
OX NCBI_TaxID=1379702 {ECO:0000313|EMBL:CDG66102.1, ECO:0000313|Proteomes:UP000017867};
RN [1] {ECO:0000313|EMBL:CDG66102.1, ECO:0000313|Proteomes:UP000017867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MB1 {ECO:0000313|Proteomes:UP000017867};
RA Maus I., Wibberg D., Stantscheff R., Cibis K., Eikmeyer F.G., Puehler A.,
RA Koenig H., Schlueter A.;
RT "Methanobacterium sp. Mb1.";
RL Submitted (JUL-2013) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; HG425166; CDG66102.1; -; Genomic_DNA.
DR AlphaFoldDB; U6EEX2; -.
DR STRING; 1379702.MBMB1_2028; -.
DR KEGG; meth:MBMB1_2028; -.
DR PATRIC; fig|1379702.4.peg.2007; -.
DR HOGENOM; CLU_006033_3_0_2; -.
DR BioCyc; MSP1379702:MBMB1_RS09870-MONOMER; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000017867; Chromosome.
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;
KW Lyase {ECO:0000313|EMBL:CDG66102.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000017867}.
FT DOMAIN 8..182
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
SQ SEQUENCE 192 AA; 21003 MW; 2D8E21F8B059A991 CRC64;
MIQKPLTKEI CEFAHYLYSN GLAPGKSGNI SVRFQDTVAI TPSGVSLGQL KENEVVLTDM
DGQVVAGGDN PSSELQLHLE IYKNKKETAG IVHTHSSYAT GFAMSGQKIE RLEGFGEISK
PFLKMVDYKP PGTMELAKLV GEGLKYEDVV ILEKHGVVAT GENLREAALL AEFIEETAKT
QFIARVLSKI EF
//
