MFNB_METS3
ID MFNB_METS3 Reviewed; 237 AA.
AC A5UNQ5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 65.
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=Msm_1628;
OS Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=420247;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35061 / DSM 861 / OCM 144 / PS;
RX PubMed=17563350; DOI=10.1073/pnas.0704189104;
RA Samuel B.S., Hansen E.E., Manchester J.K., Coutinho P.M., Henrissat B.,
RA Fulton R., Latreille P., Kim K., Wilson R.K., Gordon J.I.;
RT "Genomic and metabolic adaptations of Methanobrevibacter smithii to the
RT human gut.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10643-10648(2007).
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}.
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; CP000678; ABQ87833.1; -; Genomic_DNA.
DR RefSeq; WP_011954643.1; NC_009515.1.
DR AlphaFoldDB; A5UNQ5; -.
DR SMR; A5UNQ5; -.
DR STRING; 420247.Msm_1628; -.
DR EnsemblBacteria; ABQ87833; ABQ87833; Msm_1628.
DR GeneID; 5216862; -.
DR KEGG; msi:Msm_1628; -.
DR PATRIC; fig|420247.28.peg.1618; -.
DR eggNOG; arCOG04482; Archaea.
DR HOGENOM; CLU_068659_0_0_2; -.
DR OMA; NFPWVIR; -.
DR BioCyc; MSMI420247:GHWZ-1669-MON; -.
DR UniPathway; UPA00080; -.
DR Proteomes; UP000001992; 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 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..237
FT /note="(5-formylfuran-3-yl)methyl phosphate synthase"
FT /id="PRO_1000044923"
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 237 AA; 25250 MW; 83C83942BD89D9DB CRC64;
MLLLISPINH EEALESIKGG ADIVDVKNPK EGSLGANFPW VIRDIREITP EDKLVSATLG
DVPYKPGTVS LAAMGAHVSG ADYIKVGLYG TKDYDEAVEV MENVAKTIKD VDNDTIVVAS
GYADAHRVGA VDPMEIPKVA KDAGCDLAML DTAVKDGHTL FDYLSIEDLE KFVNEAHSYG
LKTALAGSVK KEQLKPLNDI GCDVVGIRGA ACVGGDRNTG KIHHTAVAEL KELCDSF