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Database: UniProt
Entry: C7P8V7
LinkDB: C7P8V7
Original site: C7P8V7 
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   13-FEB-2019, entry version 50.
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;
OC   Methanococcales; 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.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., 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
RT   (MfnD) involved in methanofuran biosynthesis.";
RL   Biochemistry 53:6220-6230(2014).
CC   -!- FUNCTION: Catalyzes the formation of an amide bond between
CC       tyramine and the gamma carboxy group of L-glutamate. The enzyme
CC       also accepts phenylethylamine in vitro.
CC       {ECO:0000269|PubMed:25211225}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + tyramine = ADP + gamma-L-
CC         glutamyltyramine + H(+) + phosphate; Xref=Rhea:RHEA:43544,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:83425, ChEBI:CHEBI:327995,
CC         ChEBI:CHEBI:456216; EC=6.3.4.24;
CC         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)
CC         toward 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}.
DR   EMBL; CP001696; ACV24989.1; -; Genomic_DNA.
DR   RefSeq; WP_015791725.1; NC_013156.1.
DR   ProteinModelPortal; 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   eggNOG; COG1821; LUCA.
DR   HOGENOM; HOG000254255; -.
DR   KO; K06914; -.
DR   OMA; DVNPRPT; -.
DR   OrthoDB; 58527at2157; -.
DR   BioCyc; MetaCyc:MONOMER-18939; -.
DR   BioCyc; MFER573064:G1GFN-1216-MONOMER; -.
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; Complete proteome; Ligase; Magnesium; Manganese;
KW   Metal-binding; Nucleotide-binding.
FT   CHAIN         1    291       Tyramine--L-glutamate ligase.
FT                                /FTId=PRO_0000432374.
FT   DOMAIN      104    274       ATP-grasp. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   NP_BIND     131    176       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00409}.
FT   METAL       236    236       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       247    247       Magnesium or manganese 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       247    247       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   METAL       249    249       Magnesium or manganese 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00409}.
FT   MUTAGEN      21     21       E->Q: 30% of wild-type specific activity.
FT                                {ECO:0000269|PubMed:25211225}.
FT   MUTAGEN     251    251       R->A: 1% of wild-type specific activity.
FT                                {ECO:0000269|PubMed:25211225}.
FT   MUTAGEN     253    253       T->V: 30% of wild-type specific activity.
FT                                {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
//
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