ID MFNB_METJA Reviewed; 235 AA.
AC Q58499;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=(5-formylfuran-3-yl)methyl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00681, ECO:0000305};
DE EC=4.2.3.153 {ECO:0000255|HAMAP-Rule:MF_00681, ECO:0000269|PubMed:25905665};
DE AltName: Full=4-(hydroxymethyl)-2-furancarboxaldehyde-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00681, ECO:0000303|PubMed:25905665};
DE Short=4-HFC-P synthase {ECO:0000255|HAMAP-Rule:MF_00681, ECO:0000303|PubMed:24977328};
GN Name=mfnB {ECO:0000255|HAMAP-Rule:MF_00681, ECO:0000303|PubMed:24977328};
GN OrderedLocusNames=MJ1099;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, AND PATHWAY.
RX PubMed=24977328; DOI=10.1021/bi500615p;
RA Miller D., Wang Y., Xu H., Harich K., White R.H.;
RT "Biosynthesis of the 5-(aminomethyl)-3-furanmethanol moiety of
RT methanofuran.";
RL Biochemistry 53:4635-4647(2014).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION
RP MECHANISM, PATHWAY, ACTIVE SITE, AND MUTAGENESIS OF ASP-25; LYS-27; LYS-85;
RP ASP-151 AND LYS-155.
RX PubMed=25905665; DOI=10.1021/acs.biochem.5b00176;
RA Wang Y., Jones M.K., Xu H., Ray W.K., White R.H.;
RT "Mechanism of the enzymatic synthesis of 4-(hydroxymethyl)-2-
RT furancarboxaldehyde-phosphate (4-HFC-P) from glyceraldehyde-3-phosphate
RT catalyzed by 4-HFC-P synthase.";
RL Biochemistry 54:2997-3008(2015).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), AND SUBUNIT.
RX PubMed=25372812; DOI=10.1107/s2053230x1402130x;
RA Bobik T.A., Morales E.J., Shin A., Cascio D., Sawaya M.R., Arbing M.,
RA Yeates T.O., Rasche M.E.;
RT "Structure of the methanofuran/methanopterin-biosynthetic enzyme MJ1099
RT from Methanocaldococcus jannaschii.";
RL Acta Crystallogr. F 70:1472-1479(2014).
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 ECO:0000269|PubMed:24977328, ECO:0000269|PubMed:25905665}.
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 ECO:0000269|PubMed:25905665};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 0.026 sec(-1). {ECO:0000269|PubMed:25905665};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:25905665};
CC -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00681, ECO:0000269|PubMed:24977328,
CC ECO:0000269|PubMed:25905665}.
CC -!- SUBUNIT: Homohexamer. Trimer of dimers. {ECO:0000269|PubMed:25372812}.
CC -!- SIMILARITY: Belongs to the MfnB family. {ECO:0000255|HAMAP-
CC Rule:MF_00681}.
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DR EMBL; L77117; AAB99102.1; -; Genomic_DNA.
DR PIR; B64437; B64437.
DR RefSeq; WP_010870611.1; NC_000909.1.
DR PDB; 4RC1; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I=1-235.
DR PDB; 4U9P; X-ray; 1.70 A; A/B/C=1-235.
DR PDBsum; 4RC1; -.
DR PDBsum; 4U9P; -.
DR AlphaFoldDB; Q58499; -.
DR SMR; Q58499; -.
DR STRING; 243232.MJ_1099; -.
DR PaxDb; 243232-MJ_1099; -.
DR DNASU; 1451996; -.
DR EnsemblBacteria; AAB99102; AAB99102; MJ_1099.
DR GeneID; 1451996; -.
DR KEGG; mja:MJ_1099; -.
DR eggNOG; arCOG04482; Archaea.
DR HOGENOM; CLU_068659_0_0_2; -.
DR InParanoid; Q58499; -.
DR OrthoDB; 81473at2157; -.
DR PhylomeDB; Q58499; -.
DR BioCyc; MetaCyc:MONOMER-18937; -.
DR BRENDA; 4.2.3.153; 3260.
DR UniPathway; UPA00080; -.
DR Proteomes; UP000000805; 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 CDD; cd00945; Aldolase_Class_I; 1.
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 1: Evidence at protein level;
KW 3D-structure; Lyase; Reference proteome; Schiff base.
FT CHAIN 1..235
FT /note="(5-formylfuran-3-yl)methyl phosphate synthase"
FT /id="PRO_0000134865"
FT ACT_SITE 27
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00681,
FT ECO:0000305|PubMed:25905665"
FT ACT_SITE 85
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00681,
FT ECO:0000305|PubMed:25905665"
FT MUTAGEN 25
FT /note="D->N: Lack of activity."
FT /evidence="ECO:0000269|PubMed:25905665"
FT MUTAGEN 27
FT /note="K->R: Lack of activity."
FT /evidence="ECO:0000269|PubMed:25905665"
FT MUTAGEN 85
FT /note="K->R: Lack of activity."
FT /evidence="ECO:0000269|PubMed:25905665"
FT MUTAGEN 151
FT /note="D->N: Lack of activity."
FT /evidence="ECO:0000269|PubMed:25905665"
FT MUTAGEN 155
FT /note="K->R: Almost no change in activity."
FT /evidence="ECO:0000269|PubMed:25905665"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:4U9P"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:4U9P"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:4U9P"
FT HELIX 29..31
FT /evidence="ECO:0007829|PDB:4U9P"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:4U9P"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:4U9P"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:4U9P"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:4U9P"
FT HELIX 94..111
FT /evidence="ECO:0007829|PDB:4U9P"
FT STRAND 115..122
FT /evidence="ECO:0007829|PDB:4U9P"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:4U9P"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:4U9P"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:4U9P"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:4U9P"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:4U9P"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:4U9P"
FT STRAND 182..185
FT /evidence="ECO:0007829|PDB:4U9P"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:4U9P"
FT HELIX 194..199
FT /evidence="ECO:0007829|PDB:4U9P"
FT STRAND 203..208
FT /evidence="ECO:0007829|PDB:4U9P"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:4U9P"
FT STRAND 212..214
FT /evidence="ECO:0007829|PDB:4RC1"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:4RC1"
FT HELIX 224..233
FT /evidence="ECO:0007829|PDB:4U9P"
SQ SEQUENCE 235 AA; 25099 MW; 9F425AC7C6096E85 CRC64;
MILLVSPIDV EEAKEAIAGG ADIIDVKNPK EGSLGANFPW MIKAIREVTP KDLLVSATVG
DVPYKPGTIS LAAVGAAISG ADYIKVGLYG VKNYYQAVEL MKNVVRAVKD IDENKIVVAA
GYADAYRVGA VEPLIVPKIA RDAGCDVAML DTAIKDGKTL FDFQSKEILA EFVDEAHSYG
LKCALAGSIK KEHIPILKEI GTDIVGVRGA ACKGGDRNNG RIDRELVKEL KELCK
//
