ID   MFNB_METM6              Reviewed;         236 AA.
AC   A9A7Q1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=MmarC6_0176;
OS   Methanococcus maripaludis (strain C6 / ATCC BAA-1332).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=444158;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C6 / ATCC BAA-1332;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B.,
RA   Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C6.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000867; ABX00999.1; -; Genomic_DNA.
DR   RefSeq; WP_012192984.1; NC_009975.1.
DR   AlphaFoldDB; A9A7Q1; -.
DR   SMR; A9A7Q1; -.
DR   STRING; 444158.MmarC6_0176; -.
DR   PRIDE; A9A7Q1; -.
DR   EnsemblBacteria; ABX00999; ABX00999; MmarC6_0176.
DR   GeneID; 5737797; -.
DR   KEGG; mmx:MmarC6_0176; -.
DR   eggNOG; arCOG04482; Archaea.
DR   HOGENOM; CLU_068659_0_0_2; -.
DR   OMA; NFPWVIR; -.
DR   OrthoDB; 71837at2157; -.
DR   PhylomeDB; A9A7Q1; -.
DR   UniPathway; UPA00080; -.
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   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   Pfam; PF04476; 4HFCP_synth; 1.
DR   PIRSF; PIRSF015957; UCP015957; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
PE   3: Inferred from homology;
KW   Lyase; Schiff base.
FT   CHAIN           1..236
FT                   /note="(5-formylfuran-3-yl)methyl phosphate synthase"
FT                   /id="PRO_1000131715"
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;  25171 MW;  E0A8A83FCDCE5CFD CRC64;
     MILLVSPKDV AEAYEAIEGG ADIIDVKNPP EGSLGANFPW VIKETREATP EGMLVSAAIG
     DVPYKPGTVT LAALGATVSG ADYIKVGLYG TRSYQEALDV MKNVTKAVKA VGENKIVVAA
     GYADAYRVGG VDPLVIPRVA RDAGCDVAML DTAVKDGKTL FDHMSIELLK EFVEETHKYG
     MKCALAGSIK IEEIPMLKEI NCDIVGVRGA ACTKGDRNEG RIQKDLVKEI VKVCKE