MFND_METFA
ID MFND_METFA Reviewed; 291 AA.
AC C7P8V7;
DT 04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Tyramine--L-glutamate ligase;
DE EC=6.3.4.24 {ECO:0000269|PubMed:25211225};
GN Name=mfnD {ECO:0000303|PubMed:25211225};
GN OrderedLocusNames=Mefer_1180 {ECO:0000312|EMBL:ACV24989.1};
OS Methanocaldococcus fervens (strain DSM 4213 / JCM 15782 / AG86)
OS (Methanococcus fervens).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=573064;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4213 / JCM 15782 / AG86;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Lupa-Sieprawska M., Whitman W.B.;
RT "Complete sequence of chromosome of Methanocaldococcus fervens AG86.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, COFACTOR, AND MUTAGENESIS OF GLU-21; ARG-251 AND THR-253.
RC STRAIN=DSM 4213 / JCM 15782 / AG86;
RX PubMed=25211225; DOI=10.1021/bi500879h;
RA Wang Y., Xu H., Harich K.C., White R.H.;
RT "Identification and characterization of a tyramine-glutamate ligase (MfnD)
RT involved in methanofuran biosynthesis.";
RL Biochemistry 53:6220-6230(2014).
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:0000269|PubMed:25211225}.
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:0000269|PubMed:25211225};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:25211225};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:25211225};
CC Note=Binds 2 magnesium or manganese ions per subunit.
CC {ECO:0000255|PROSITE-ProRule:PRU00409};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.8 mM for tyramine {ECO:0000269|PubMed:25211225};
CC KM=2.3 mM for L-glutamate {ECO:0000269|PubMed:25211225};
CC KM=1.5 mM for ATP {ECO:0000269|PubMed:25211225};
CC Note=kcat is 4.8 sec(-1) toward tyramine. kcat is 5.8 sec(-1) toward
CC L-glutamate. kcat is 5.9 sec(-1) toward ATP.
CC {ECO:0000269|PubMed:25211225};
CC pH dependence:
CC Optimum pH is 6.7. {ECO:0000269|PubMed:25211225};
CC -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis.
CC {ECO:0000305|PubMed:25211225}.
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DR EMBL; CP001696; ACV24989.1; -; Genomic_DNA.
DR RefSeq; WP_015791725.1; NC_013156.1.
DR AlphaFoldDB; C7P8V7; -.
DR SMR; C7P8V7; -.
DR STRING; 573064.Mefer_1180; -.
DR EnsemblBacteria; ACV24989; ACV24989; Mefer_1180.
DR GeneID; 8365882; -.
DR KEGG; mfe:Mefer_1180; -.
DR eggNOG; arCOG01592; Archaea.
DR HOGENOM; CLU_059501_1_1_2; -.
DR OMA; DVNPRPT; -.
DR OrthoDB; 58527at2157; -.
DR BioCyc; MetaCyc:MON-18939; -.
DR BRENDA; 6.3.4.24; 12857.
DR UniPathway; UPA00080; -.
DR Proteomes; UP000001495; 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 InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR003806; ATP-grasp_PylC-type.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR024710; MfnD.
DR InterPro; IPR040803; MfnD_preATP-grasp.
DR Pfam; PF02655; ATP-grasp_3; 1.
DR Pfam; PF18301; preATP-grasp_3; 1.
DR PIRSF; PIRSF016766; UCP016766_ATPgrasp; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Magnesium; Manganese; Metal-binding;
KW Nucleotide-binding.
FT CHAIN 1..291
FT /note="Tyramine--L-glutamate ligase"
FT /id="PRO_0000432374"
FT DOMAIN 104..274
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 131..176
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 236
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 247
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 249
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 249
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT MUTAGEN 21
FT /note="E->Q: 30% of wild-type specific activity."
FT /evidence="ECO:0000269|PubMed:25211225"
FT MUTAGEN 251
FT /note="R->A: 1% of wild-type specific activity."
FT /evidence="ECO:0000269|PubMed:25211225"
FT MUTAGEN 253
FT /note="T->V: 30% of wild-type specific activity."
FT /evidence="ECO:0000269|PubMed:25211225"
SQ SEQUENCE 291 AA; 33289 MW; 02750565759370CB CRC64;
MILFFEYAIA SGFEDEGILE EGKMMFNTLL NQFLEIDNVT SLIHKDFADD YKDFENLKIV
EIEDDKDIEI KLNDILKNEK IDYALTIAPE DENILYNLTK IIEKYPVKNL GCSSNAIKVA
GDKYLTYLTI KDYVKTPKTF KPKKYVIKKI DGCGGKFNLF DENFLIQEFV EGESLSVSLI
VGKKIYPLSL NRQYIDERGF VGGEVNIKHR LKDEIFNEAI KAVKCIDGLN GYVGVDVIVN
DEIYIIEINP RITTTIYGLK TEPSLAELLI KNANNEELTF KVEGKEFTIN K
