ID   MFNF_METVA              Reviewed;         222 AA.
AC   Q50834;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=(4-{4-[2-(gamma-L-glutamylamino)ethyl]phenoxymethyl}furan-2-yl)methanamine synthase {ECO:0000250|UniProtKB:Q58250};
DE            EC=2.5.1.131 {ECO:0000250|UniProtKB:Q58250};
DE   AltName: Full=4-[[4-(2-aminoethyl)phenoxy]-methyl]-2-furanmethanamine-glutamate synthase {ECO:0000250|UniProtKB:Q58250};
DE            Short=APMF-Glu synthase {ECO:0000250|UniProtKB:Q58250};
DE   Flags: Fragment;
GN   Name=mfnF {ECO:0000250|UniProtKB:Q58250};
OS   Methanococcus vannielii.
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=2187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3133361; DOI=10.1128/jb.170.7.3125-3130.1988;
RA   Morris C.J., Reeve J.N.;
RT   "Conservation of structure in the human gene encoding argininosuccinate
RT   synthetase and the argG genes of the archaebacteria Methanosarcina barkeri
RT   MS and Methanococcus vannielii.";
RL   J. Bacteriol. 170:3125-3130(1988).
CC   -!- FUNCTION: Catalyzes the condensation between 5-(aminomethyl)-3-
CC       furanmethanol diphosphate (F1-PP) and gamma-glutamyltyramine to produce
CC       APMF-Glu. {ECO:0000250|UniProtKB:Q58250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[5-(aminomethyl)furan-3-yl]methyl diphosphate + gamma-L-
CC         glutamyltyramine = (4-{4-[2-(gamma-L-
CC         glutamylamino)ethyl]phenoxymethyl}furan-2-yl)methanamine +
CC         diphosphate; Xref=Rhea:RHEA:47840, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:83425, ChEBI:CHEBI:88054, ChEBI:CHEBI:88055;
CC         EC=2.5.1.131; Evidence={ECO:0000250|UniProtKB:Q58250};
CC   -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis.
CC       {ECO:0000250|UniProtKB:Q58250}.
CC   -!- SIMILARITY: Belongs to the MfnF family. {ECO:0000305}.
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; M21315; AAA88321.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q50834; -.
DR   SMR; Q50834; -.
DR   UniPathway; UPA00080; -.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR002821; Hydantoinase_A.
DR   Pfam; PF01968; Hydantoinase_A; 1.
PE   3: Inferred from homology;
KW   Transferase.
FT   CHAIN           <1..222
FT                   /note="(4-{4-[2-(gamma-L-
FT                   glutamylamino)ethyl]phenoxymethyl}furan-2-yl)methanamine
FT                   synthase"
FT                   /id="PRO_0000107077"
FT   NON_TER         1
SQ   SEQUENCE   222 AA;  24655 MW;  2AA3DC7D3A0105DE CRC64;
     AEFVSQNIDK NCILVDMGST TTDIIPIVDG KAASNKTDLE RLMNNELLYV GSLRTPLSFL
     SNKIMFKDTI TNVSSEYFAI TGDISLVLDK ITEMDYSCDT PDGKPADKRN SLIRISKVLC
     SDLNQISADE SINIAIEYYK ILIDLILENV KKVSEKYGLK NIVITGLGEE ILKDALSELT
     KSNEFNIISI KERYGKDVSL ATPSFSVSIL LKNELNAKLN RS