ID MFND_METJA Reviewed; 308 AA.
AC Q58225;
DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=Tyramine--L-glutamate ligase;
DE EC=6.3.4.24 {ECO:0000250|UniProtKB:C7P8V7};
GN Name=mfnD; OrderedLocusNames=MJ0815;
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).
CC -!- FUNCTION: Catalyzes the formation of an amide bond between tyramine and
CC the gamma carboxy group of L-glutamate. The enzyme also accepts
CC phenylethylamine in vitro. {ECO:0000250|UniProtKB:C7P8V7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + tyramine = ADP + gamma-L-glutamyltyramine
CC + H(+) + phosphate; Xref=Rhea:RHEA:43544, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83425, ChEBI:CHEBI:327995, ChEBI:CHEBI:456216;
CC EC=6.3.4.24; Evidence={ECO:0000250|UniProtKB:C7P8V7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:C7P8V7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:C7P8V7};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00409};
CC -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis.
CC {ECO:0000250|UniProtKB:C7P8V7}.
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DR EMBL; L77117; AAB98814.1; -; Genomic_DNA.
DR PIR; G64401; G64401.
DR AlphaFoldDB; Q58225; -.
DR SMR; Q58225; -.
DR STRING; 243232.MJ_0815; -.
DR PaxDb; 243232-MJ_0815; -.
DR EnsemblBacteria; AAB98814; AAB98814; MJ_0815.
DR KEGG; mja:MJ_0815; -.
DR eggNOG; arCOG01592; Archaea.
DR HOGENOM; CLU_059501_1_1_2; -.
DR InParanoid; Q58225; -.
DR PhylomeDB; Q58225; -.
DR UniPathway; UPA00080; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 2.30.36.100; -; 1.
DR Gene3D; 3.40.50.11770; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR003806; ATP-grasp_PylC-type.
DR InterPro; IPR024710; MfnD.
DR InterPro; IPR040803; MfnD_preATP-grasp.
DR NCBIfam; NF040722; MfnD_Meth; 1.
DR Pfam; PF02655; ATP-grasp_3; 1.
DR Pfam; PF18301; preATP-grasp_3; 1.
DR PIRSF; PIRSF016766; UCP016766_ATPgrasp; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..308
FT /note="Tyramine--L-glutamate ligase"
FT /id="PRO_0000013998"
FT DOMAIN 89..291
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 115..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 252
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 252
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 264
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 264
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 264
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 266
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
SQ SEQUENCE 308 AA; 35061 MW; 08C458E046749061 CRC64;
MLLLQSILIT KIMVIQLILF FEYALASGFE DKNILKEGKM MFDTLLKQFL EIDKVISLLY
KDFVDNYIDF KNLEIVKIKK ENEIENKLKS LLKSENIDYA LVVAPEDEDI LYNLTKIIES
YPVKNLGCSS EAIKIAGNKY LTYLAIKDAV KTPKTFPPKK YVVKKIDSCG GKFNLFDENF
LIQEFIDGEN LSVSLIVGKK IHPLSLNRQY IDKRGFVGGE VNINHKLKDK IFNEAIKAVK
CINGLNGYVG VDVIVNNDGI YIIEINPRIT TTIYGLKTNP SLAELLIKNA NNEELKFKVK
GEKFTIDK
//
