MFNE_METJA
ID MFNE_METJA Reviewed; 216 AA.
AC Q57900;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=[5-(aminomethyl)furan-3-yl]methyl phosphate kinase {ECO:0000305};
DE EC=2.7.4.31 {ECO:0000269|PubMed:26100040};
DE AltName: Full=5-(aminomethyl)-3-furanmethanol phosphate kinase {ECO:0000305};
GN Name=mfnE {ECO:0000303|PubMed:26100040};
GN Synonyms=adkB {ECO:0000303|PubMed:22002406}; OrderedLocusNames=MJ0458;
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 AS AN ADENYLATE KINASE, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=22002406; DOI=10.1007/s00203-011-0759-9;
RA Grochowski L.L., Censky K., Xu H., White R.H.;
RT "A new class of adenylate kinase in methanogens is related to uridylate
RT kinase.";
RL Arch. Microbiol. 194:141-145(2012).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, 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).
RN [4]
RP CRYSTALLIZATION.
RX PubMed=24192367; DOI=10.1107/s1744309113026638;
RA Wang X., Yuan Y., Teng M., Niu L., Gao Y.;
RT "Crystallization and preliminary X-ray diffraction analysis of MJ0458, an
RT adenylate kinase from Methanocaldococcus jannaschii.";
RL Acta Crystallogr. F 69:1272-1274(2013).
CC -!- FUNCTION: Catalyzes the formation of 5-(aminomethyl)-3-furanmethanol
CC diphosphate (F1-PP) from 5-(aminomethyl)-3-furanmethanol phosphate (F1-
CC P) and ATP (PubMed:26100040). In vitro, can also act as an adenylate
CC kinase that catalyzes the transfer of a phosphoryl group from ATP to
CC AMP, generating two molecules of ADP (PubMed:22002406).
CC {ECO:0000269|PubMed:22002406, ECO:0000269|PubMed:26100040}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[5-(aminomethyl)-3-furyl]methyl phosphate + ATP = [5-
CC (aminomethyl)furan-3-yl]methyl diphosphate + ADP;
CC Xref=Rhea:RHEA:47836, ChEBI:CHEBI:30616, ChEBI:CHEBI:83431,
CC ChEBI:CHEBI:88054, ChEBI:CHEBI:456216; EC=2.7.4.31;
CC Evidence={ECO:0000269|PubMed:26100040};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:26100040};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:26100040}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10.2 uM for ATP {ECO:0000269|PubMed:22002406};
CC KM=26.2 uM for AMP {ECO:0000269|PubMed:22002406};
CC Vmax=3.1 umol/min/mg enzyme for the adenylate kinase reaction (at 37
CC degrees Celsius) {ECO:0000269|PubMed:22002406};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:26100040};
CC -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis.
CC {ECO:0000305|PubMed:26100040}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:22002406}.
CC -!- SIMILARITY: Belongs to the MfnE family. {ECO:0000305}.
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DR EMBL; L77117; AAB98446.1; -; Genomic_DNA.
DR PIR; B64357; B64357.
DR RefSeq; WP_010869957.1; NC_000909.1.
DR AlphaFoldDB; Q57900; -.
DR SMR; Q57900; -.
DR STRING; 243232.MJ_0458; -.
DR EnsemblBacteria; AAB98446; AAB98446; MJ_0458.
DR GeneID; 1451319; -.
DR KEGG; mja:MJ_0458; -.
DR eggNOG; arCOG00859; Archaea.
DR HOGENOM; CLU_089197_0_0_2; -.
DR InParanoid; Q57900; -.
DR OMA; LPHSWDV; -.
DR OrthoDB; 85553at2157; -.
DR PhylomeDB; Q57900; -.
DR BioCyc; MetaCyc:MON-19567; -.
DR BRENDA; 2.7.4.3; 3260.
DR BRENDA; 2.7.4.31; 3260.
DR UniPathway; UPA00080; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04240; AAK_UC; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR011375; MfnE.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF004857; Kin_aa_kin; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..216
FT /note="[5-(aminomethyl)furan-3-yl]methyl phosphate kinase"
FT /id="PRO_0000106886"
FT BINDING 5..9
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HLX1"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HLX1"
FT BINDING 142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HLX1"
FT BINDING 147..152
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HLX1"
FT BINDING 166
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9HLX1"
SQ SEQUENCE 216 AA; 24080 MW; 37856E333F3D2A76 CRC64;
MHIVKIGGSL TYDAKPLLKA LKNYAKENNK KIVIIPGGGE FANVVRKIDK ALNISNSLSH
KLAIKCMDLI GEVYAEIGYI KAYDTLFDLK REIEKEKIAI LLPSKILLST DIAEHSWAIT
SDSLSLYIGK LLDVREVIIA TDVDGIYDKF PGGKLLNIIN ANDIKGLTSV DETFPILLKQ
FKMNAYVVNG RHPERVMDIL EGKHNIYTKI VGIDKI
