GenomeNet

Database: UniProt
Entry: A0A0E3NNC3_9EURY
LinkDB: A0A0E3NNC3_9EURY
Original site: A0A0E3NNC3_9EURY 
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
//
DBGET integrated database retrieval system