ID E3GXG6_METFV Unreviewed; 237 AA.
AC E3GXG6;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=(5-formylfuran-3-yl)methyl phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00681};
DE EC=4.2.3.153 {ECO:0000256|HAMAP-Rule:MF_00681};
DE AltName: Full=4-(hydroxymethyl)-2-furancarboxaldehyde-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00681};
DE Short=4-HFC-P synthase {ECO:0000256|HAMAP-Rule:MF_00681};
GN Name=mfnB {ECO:0000256|HAMAP-Rule:MF_00681};
GN OrderedLocusNames=Mfer_0195 {ECO:0000313|EMBL:ADP76998.1};
OS Methanothermus fervidus (strain ATCC 43054 / DSM 2088 / JCM 10308 / V24 S).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanothermaceae; Methanothermus.
OX NCBI_TaxID=523846 {ECO:0000313|EMBL:ADP76998.1, ECO:0000313|Proteomes:UP000002315};
RN [1] {ECO:0000313|EMBL:ADP76998.1, ECO:0000313|Proteomes:UP000002315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43054 / DSM 2088 / JCM 10308 / V24 S
RC {ECO:0000313|Proteomes:UP000002315};
RX PubMed=21304736;
RA Anderson I., Djao O.D., Misra M., Chertkov O., Nolan M., Lucas S.,
RA Lapidus A., Del Rio T.G., Tice H., Cheng J.F., Tapia R., Han C.,
RA Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA Mikhailova N., Pati A., Brambilla E., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Sikorski J., Spring S., Rohde M.,
RA Eichinger K., Huber H., Wirth R., Goker M., Detter J.C., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Methanothermus fervidus type strain (V24S).";
RL Stand. Genomic Sci. 3:315-324(2010).
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:0000256|ARBA:ARBA00003810,
CC ECO:0000256|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:0000256|ARBA:ARBA00001294, ECO:0000256|HAMAP-
CC Rule:MF_00681};
CC -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_00681}.
CC -!- SIMILARITY: Belongs to the MfnB family. {ECO:0000256|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; CP002278; ADP76998.1; -; Genomic_DNA.
DR RefSeq; WP_013413276.1; NC_014658.1.
DR AlphaFoldDB; E3GXG6; -.
DR STRING; 523846.Mfer_0195; -.
DR GeneID; 9961908; -.
DR KEGG; mfv:Mfer_0195; -.
DR HOGENOM; CLU_068659_0_0_2; -.
DR OrthoDB; 81473at2157; -.
DR UniPathway; UPA00080; -.
DR Proteomes; UP000002315; 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 Pfam; PF04476; 4HFCP_synth; 1.
DR PIRSF; PIRSF015957; UCP015957; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00681};
KW Reference proteome {ECO:0000313|Proteomes:UP000002315};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_00681}.
FT ACT_SITE 27
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00681,
FT ECO:0000256|PIRSR:PIRSR015957-1"
FT ACT_SITE 85
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00681,
FT ECO:0000256|PIRSR:PIRSR015957-1"
SQ SEQUENCE 237 AA; 25285 MW; 5400242C31D43FCF CRC64;
MLLLVSPINT KEAKEAIEGG ADIIDVKNPK EGSLGANFPW VIKSIKEIIP KDKLLSATVG
DIDYKPGTVS LAVLGAVTSG ADYVKIGLYG TKNYEQALEV MKNAVKTVEY SESEAFVVAA
GYGDAKRVNS VDPMEIPNIA ADADADVAML DTAIKDGKCL LDFLNLNELA EFVENSHDHG
LKCALAGSLK KEHVKLLHEI GCDIVGIRGA ACIGGDRNKG YIHRSAVSEL KNIIKGF
//
