MFNB_METBF
ID MFNB_METBF Reviewed; 234 AA.
AC Q46DH3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=Mbar_A1101;
OS Methanosarcina barkeri (strain Fusaro / DSM 804).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=269797;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fusaro / DSM 804;
RX PubMed=16980466; DOI=10.1128/jb.00810-06;
RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT "The Methanosarcina barkeri genome: comparative analysis with
RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT rearrangement within methanosarcinal genomes.";
RL J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ70069.1; -; Genomic_DNA.
DR RefSeq; WP_011306117.1; NC_007355.1.
DR AlphaFoldDB; Q46DH3; -.
DR SMR; Q46DH3; -.
DR STRING; 269797.Mbar_A1101; -.
DR EnsemblBacteria; AAZ70069; AAZ70069; Mbar_A1101.
DR GeneID; 3627512; -.
DR KEGG; mba:Mbar_A1101; -.
DR eggNOG; arCOG04482; Archaea.
DR HOGENOM; CLU_068659_0_0_2; -.
DR OMA; NFPWVIR; -.
DR OrthoDB; 71837at2157; -.
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 Pfam; PF04476; 4HFCP_synth; 1.
DR PIRSF; PIRSF015957; UCP015957; 1.
PE 3: Inferred from homology;
KW Lyase; Schiff base.
FT CHAIN 1..234
FT /note="(5-formylfuran-3-yl)methyl phosphate synthase"
FT /id="PRO_1000044919"
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 234 AA; 24965 MW; 09DD431C3A2809B2 CRC64;
MKLLISPINK EEAIIASRGG ADIVDVKNPK EGSLGANFPW VIRDVKGAVN GRQPISATIG
DFNYKPGTAS LAAFGAAVAG ADYIKVGLYD IQTEDQALEL ITKITQAVKD YDSTKKVVAS
GYSDYKRINS ISPLLLPSIA AKAGADVVMV DTGIKDGKST FEFMDEEELK KFTGLAHECG
LENAIAGSLK FEDLPVLERI GPDIIGVRGM VCGGDRTNSI RQELVEKLVA ECQA
