MFNB_METMP
ID MFNB_METMP Reviewed; 236 AA.
AC Q6LZC1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=(5-formylfuran-3-yl)methyl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00681};
DE EC=4.2.3.153 {ECO:0000255|HAMAP-Rule:MF_00681};
DE AltName: Full=4-(hydroxymethyl)-2-furancarboxaldehyde-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00681};
DE Short=4-HFC-P synthase {ECO:0000255|HAMAP-Rule:MF_00681};
GN Name=mfnB {ECO:0000255|HAMAP-Rule:MF_00681}; OrderedLocusNames=MMP0708;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
CC -!- FUNCTION: Catalyzes the formation of 4-(hydroxymethyl)-2-
CC furancarboxaldehyde phosphate (4-HFC-P) from two molecules of
CC glyceraldehyde-3-P (GA-3-P). {ECO:0000255|HAMAP-Rule:MF_00681}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 D-glyceraldehyde 3-phosphate = 4-(hydroxymethyl)-2-
CC furancarboxaldehyde phosphate + 2 H2O + phosphate;
CC Xref=Rhea:RHEA:43536, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:59776, ChEBI:CHEBI:83407; EC=4.2.3.153;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00681};
CC -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00681}.
CC -!- SIMILARITY: Belongs to the MfnB family. {ECO:0000255|HAMAP-
CC Rule:MF_00681}.
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DR EMBL; BX950229; CAF30264.1; -; Genomic_DNA.
DR RefSeq; WP_011170652.1; NC_005791.1.
DR AlphaFoldDB; Q6LZC1; -.
DR SMR; Q6LZC1; -.
DR STRING; 267377.MMP0708; -.
DR EnsemblBacteria; CAF30264; CAF30264; MMP0708.
DR GeneID; 41279177; -.
DR KEGG; mmp:MMP0708; -.
DR PATRIC; fig|267377.15.peg.725; -.
DR eggNOG; arCOG04482; Archaea.
DR HOGENOM; CLU_068659_0_0_2; -.
DR OMA; NFPWVIR; -.
DR OrthoDB; 71837at2157; -.
DR BioCyc; MMAR267377:MMP_RS03705-MON; -.
DR UniPathway; UPA00080; -.
DR Proteomes; UP000000590; Chromosome.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:2001120; P:methanofuran biosynthetic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00681; MfnB; 1.
DR InterPro; IPR007565; 4HFCP_synth.
DR InterPro; IPR035081; 4HFCP_synth_arc.
DR Pfam; PF04476; 4HFCP_synth; 1.
DR PIRSF; PIRSF015957; UCP015957; 1.
PE 3: Inferred from homology;
KW Lyase; Reference proteome; Schiff base.
FT CHAIN 1..236
FT /note="(5-formylfuran-3-yl)methyl phosphate synthase"
FT /id="PRO_1000044922"
FT ACT_SITE 27
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00681"
FT ACT_SITE 85
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00681"
SQ SEQUENCE 236 AA; 25114 MW; 0617D1B7CDCA05F7 CRC64;
MILLVSPKDV AEAYEAIEGG ADIIDVKNPP EGSLGANFPW VIKETREATP EGMLVSAAIG
DVPYKPGTVT LAALGATVSG ADYIKVGLYG TRSYQEALDV MKNVTKAVKD AGENKIVVAA
GYADAYRVGA VDPLVIPKVA RDAGCDVAML DTAVKDGKTL FDHMDLDLLR EFVEETHKYG
MKCALAGSIK IEEIPMLKEI GCDIVGVRGA ACTQGDRNAG RIQKDLVKEI VKVCRD