ID   GMAS_METUF              Reviewed;         442 AA.
AC   F5RH07; D7R618;
DT   04-FEB-2015, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Glutamate--methylamine ligase {ECO:0000303|PubMed:19943898};
DE            EC=6.3.4.12 {ECO:0000269|PubMed:19943898};
DE   AltName: Full=Gamma-glutamylmethylamide synthetase {ECO:0000303|PubMed:19943898};
DE            Short=GMAS {ECO:0000303|PubMed:19943898};
GN   Name=gms {ECO:0000303|PubMed:19943898};
GN   ORFNames=METUNv1_03599 {ECO:0000312|EMBL:EGK70211.1};
OS   Methyloversatilis universalis (strain ATCC BAA-1314 / JCM 13912 / FAM5).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Sterolibacteriaceae; Methyloversatilis.
OX   NCBI_TaxID=1000565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC BAA-1314 / JCM 13912 / FAM5;
RX   PubMed=19943898; DOI=10.1111/j.1365-2958.2009.06989.x;
RA   Latypova E., Yang S., Wang Y.S., Wang T., Chavkin T.A., Hackett M.,
RA   Schafer H., Kalyuzhnaya M.G.;
RT   "Genetics of the glutamate-mediated methylamine utilization pathway in the
RT   facultative methylotrophic beta-proteobacterium Methyloversatilis
RT   universalis FAM5.";
RL   Mol. Microbiol. 75:426-439(2010).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1314 / JCM 13912 / FAM5;
RX   PubMed=21725020; DOI=10.1128/jb.05331-11;
RA   Kittichotirat W., Good N.M., Hall R., Bringel F., Lajus A., Medigue C.,
RA   Smalley N.E., Beck D., Bumgarner R., Vuilleumier S., Kalyuzhnaya M.G.;
RT   "Genome sequence of Methyloversatilis universalis FAM5T, a methylotrophic
RT   representative of the order Rhodocyclales.";
RL   J. Bacteriol. 193:4541-4542(2011).
CC   -!- FUNCTION: Catalyzes the formation of N(5)-methyl-L-glutamine from
CC       glutamate and methylamine. {ECO:0000269|PubMed:19943898}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-glutamate + methylamine = ADP + H(+) + N(5)-methyl-L-
CC         glutamine + phosphate; Xref=Rhea:RHEA:17117, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58200, ChEBI:CHEBI:59338, ChEBI:CHEBI:456216;
CC         EC=6.3.4.12; Evidence={ECO:0000269|PubMed:19943898};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:19943898};
CC       Note=No activity is detected with Mn(2+).
CC       {ECO:0000269|PubMed:19943898};
CC   -!- INDUCTION: Induced during growth on methylamine.
CC       {ECO:0000269|PubMed:19943898}.
CC   -!- DISRUPTION PHENOTYPE: Fails to grow on methylamine. N(5)-methyl-L-
CC       glutamine is not detected in the intracellular pool of free amino acids
CC       from the deletion mutant. {ECO:0000269|PubMed:19943898}.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family. Type 3
CC       subfamily. {ECO:0000305}.
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DR   EMBL; HM037347; ADH10360.1; -; Genomic_DNA.
DR   EMBL; AFHG01000058; EGK70211.1; -; Genomic_DNA.
DR   RefSeq; WP_008064112.1; NZ_AFHG01000058.1.
DR   AlphaFoldDB; F5RH07; -.
DR   SMR; F5RH07; -.
DR   STRING; 1000565.METUNv1_03599; -.
DR   EnsemblBacteria; EGK70211; EGK70211; METUNv1_03599.
DR   eggNOG; COG0174; Bacteria.
DR   OrthoDB; 416474at2; -.
DR   BRENDA; 6.3.4.12; 9966.
DR   Proteomes; UP000005019; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:InterPro.
DR   GO; GO:0047943; F:glutamate-methylamine ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.10.20.70; -; 1.
DR   InterPro; IPR036651; Gln_synt_N.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR008146; Gln_synth_cat_dom.
DR   InterPro; IPR027303; Gln_synth_gly_rich_site.
DR   InterPro; IPR017536; Glutamine_synthetase_typeIII.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF54368; SSF54368; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   TIGRFAMs; TIGR03105; gln_synth_III; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
DR   PROSITE; PS51986; GS_BETA_GRASP; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Ligase; Magnesium; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..442
FT                   /note="Glutamate--methylamine ligase"
FT                   /id="PRO_0000431890"
FT   DOMAIN          13..97
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT   DOMAIN          103..442
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ   SEQUENCE   442 AA;  48798 MW;  ACF6E605F250CA71 CRC64;
     MSPSEAQQFL KENQVKYILA QFVDIHGSAK TKSVPAEHYK TVVTDGAGFA GFAIWGMGMT
     PNVDADYMAV GDASTLSLVP WQPGYARIAC DGHTHGKPHE YDTRVVLKKQ LEQITARGWT
     FFTGMEPEFS LLRKVEGKLL PADPGDTLSK PCYDYKGLSR ARVFLERLSE SLRSVGIDVY
     QIDHEDANGQ FEINYTFTDA LTSCDHYTFF KMGAAEIAAE LGLICSFMPK PFSNRPGNGL
     HMHMSIGDGK RNLFEDKSDK HGLALSKLAY HWAAGLLKHA PALAALCCPT VNSYKRLVVG
     RSLTGATWAP AYICYGGNNR SGMIRSPGGR LELRLPDASC NAYLATAAVI AAGMDGVINE
     LDPGAPQNDN LYEYSQAQLD AAGIKVLPQN LHEALLALEK DEVIRSALGP VVDEFLRLKH
     MEWVEYMRHV SDWEVNSYLE FF