ID A0A0E3NNC3_9EURY Unreviewed; 196 AA.
AC A0A0E3NNC3;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=MSWH1_0184 {ECO:0000313|EMBL:AKB20455.1};
OS Methanosarcina sp. WH1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=1434102 {ECO:0000313|EMBL:AKB20455.1, ECO:0000313|Proteomes:UP000033112};
RN [1] {ECO:0000313|EMBL:AKB20455.1, ECO:0000313|Proteomes:UP000033112}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH1 {ECO:0000313|EMBL:AKB20455.1,
RC ECO:0000313|Proteomes:UP000033112};
RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT "Methanogenic archaea and the global carbon cycle.";
RL Submitted (JUL-2014) 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 -!- 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; CP009504; AKB20455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E3NNC3; -.
DR KEGG; mef:MSWH1_0184; -.
DR PATRIC; fig|1434102.4.peg.219; -.
DR HOGENOM; CLU_006033_3_4_2; -.
DR UniPathway; UPA00071; -.
DR Proteomes; UP000033112; 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;
FT DOMAIN 13..187
FT /note="Class II aldolase/adducin N-terminal"
FT /evidence="ECO:0000259|SMART:SM01007"
SQ SEQUENCE 196 AA; 21251 MW; 8B20C0A1445093D1 CRC64;
MAFFLYISHK MWQEMAKYGR KLVEHGLVES NFGNISVRIG DQMLITRSGT ALDEISGDNV
VEVEIQDTSS LDIIASSETV VHREIYRQTS ALAIIHAHCP YAVVESLLAG PGGVIVPVDS
EGQYFLGDIP VVGGGIGSRE LAENLAAGLS KHKGAVVYSH GTFAIGRTLG EAYIVTTQLE
HSCRIKYLYE LAAVKK
//