MFNF_METJA
ID MFNF_METJA Reviewed; 330 AA.
AC Q58250;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=(4-{4-[2-(gamma-L-glutamylamino)ethyl]phenoxymethyl}furan-2-yl)methanamine synthase {ECO:0000305};
DE EC=2.5.1.131 {ECO:0000269|PubMed:26100040};
DE AltName: Full=4-[[4-(2-aminoethyl)phenoxy]-methyl]-2-furanmethanamine-glutamate synthase {ECO:0000305};
DE Short=APMF-Glu synthase {ECO:0000305};
GN Name=mfnF {ECO:0000303|PubMed:26100040}; OrderedLocusNames=MJ0840;
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, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=26100040; DOI=10.1128/jb.00401-15;
RA Wang Y., Xu H., Jones M.K., White R.H.;
RT "Identification of the final two genes functioning in methanofuran
RT biosynthesis in Methanocaldococcus jannaschii.";
RL J. Bacteriol. 197:2850-2858(2015).
CC -!- FUNCTION: Catalyzes the condensation between 5-(aminomethyl)-3-
CC furanmethanol diphosphate (F1-PP) and gamma-glutamyltyramine to produce
CC APMF-Glu. {ECO:0000269|PubMed:26100040}.
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:0000269|PubMed:26100040};
CC -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis.
CC {ECO:0000305|PubMed:26100040}.
CC -!- SIMILARITY: Belongs to the MfnF family. {ECO:0000305}.
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DR EMBL; L77117; AAB98845.1; -; Genomic_DNA.
DR PIR; H64404; H64404.
DR AlphaFoldDB; Q58250; -.
DR SMR; Q58250; -.
DR STRING; 243232.MJ_0840; -.
DR EnsemblBacteria; AAB98845; AAB98845; MJ_0840.
DR KEGG; mja:MJ_0840; -.
DR eggNOG; arCOG04369; Archaea.
DR HOGENOM; CLU_060932_0_0_2; -.
DR InParanoid; Q58250; -.
DR OMA; TDCFADR; -.
DR PhylomeDB; Q58250; -.
DR BioCyc; MetaCyc:MON-19568; -.
DR BRENDA; 2.5.1.131; 3260.
DR UniPathway; UPA00080; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR002821; Hydantoinase_A.
DR InterPro; IPR002756; MfnF.
DR Pfam; PF01968; Hydantoinase_A; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
DR TIGRFAMs; TIGR03123; one_C_unchar_1; 1.
PE 1: Evidence at protein level;
KW Reference proteome; Transferase.
FT CHAIN 1..330
FT /note="(4-{4-[2-(gamma-L-
FT glutamylamino)ethyl]phenoxymethyl}furan-2-yl)methanamine
FT synthase"
FT /id="PRO_0000107076"
SQ SEQUENCE 330 AA; 37377 MW; 5A3EAA6D2125D829 CRC64;
MKIMILGIDI GGANTKITEI EGDNYKIHHI YFPMWKKKDE LEDLLKNYND NVDYVALVMT
AELADCYKTK KEGVEDIIDK VEKAFNCPVY VFDVNGNFLT SEEAKKNYLD VSASNWNATA
KFVAEFIKDS CILVDMGSTT TDIIPIKDKE VLAEKTDLDR LMNNQLVYVG TLRTPVSFLA
NKIEFRGKLT NLSSEYFAIT ADISLILNKI TEEDYTCDTP DGAGKDFESC LTRLVRVLCA
DREMVKDDEL IDFANKLYNK LLELIRENVD TIAKRYNLND VVITGLGEEI LKDALDEYNI
ISIKETYGKD VSLATPSFAV AKLLQKQLDK