ID MFNB_ARCFU Reviewed; 235 AA.
AC O28087;
DT 19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 103.
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=AF_2196;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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; AE000782; AAB89060.1; -; Genomic_DNA.
DR PIR; D69524; D69524.
DR RefSeq; WP_010879685.1; NC_000917.1.
DR AlphaFoldDB; O28087; -.
DR SMR; O28087; -.
DR STRING; 224325.AF_2196; -.
DR PaxDb; 224325-AF_2196; -.
DR EnsemblBacteria; AAB89060; AAB89060; AF_2196.
DR GeneID; 24795945; -.
DR KEGG; afu:AF_2196; -.
DR eggNOG; arCOG04482; Archaea.
DR HOGENOM; CLU_068659_0_0_2; -.
DR OrthoDB; 81473at2157; -.
DR PhylomeDB; O28087; -.
DR UniPathway; UPA00080; -.
DR Proteomes; UP000002199; 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; SSF51569; Aldolase; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
PE 3: Inferred from homology;
KW Lyase; Reference proteome; Schiff base.
FT CHAIN 1..235
FT /note="(5-formylfuran-3-yl)methyl phosphate synthase"
FT /id="PRO_0000134863"
FT ACT_SITE 27
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00681"
FT ACT_SITE 86
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00681"
SQ SEQUENCE 235 AA; 24939 MW; 935EA0194A6779CE CRC64;
MKVLVSPMSV AEAIEAIEGG ADIIDVKNPA EGSLGANFPW VIREISELAK KYGKEISATT
GDMPYKPGTA SLAALGAAVA GADYIKVGLY GVKNAEEAYE MMVGVVRAVK DFDSSKKVVA
AGYGDYYRIS SVSPLDLPEA VAKAGADIVM VDTAIKDGTS LFDHMKIGDI ESFVKLARDN
GLMVALAGNI SWNHIETLKE LSPDIIGVRS IVCEGDRSSM IKRELVVKLM EAVHG
//
