ID B1Z988_METPB Unreviewed; 348 AA.
AC B1Z988;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Glutamine synthetase {ECO:0000256|ARBA:ARBA00012937, ECO:0000256|RuleBase:RU004356};
DE EC=6.3.1.2 {ECO:0000256|ARBA:ARBA00012937, ECO:0000256|RuleBase:RU004356};
GN OrderedLocusNames=Mpop_2332 {ECO:0000313|EMBL:ACB80494.1};
OS Methylorubrum populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001)
OS (Methylobacterium populi).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=441620 {ECO:0000313|EMBL:ACB80494.1, ECO:0000313|Proteomes:UP000007136};
RN [1] {ECO:0000313|EMBL:ACB80494.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJ001 {ECO:0000313|EMBL:ACB80494.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marx C., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium populi BJ001.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from
CC glutamate and ammonia. {ECO:0000256|ARBA:ARBA00003117}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate + NH4(+) = ADP + H(+) + L-glutamine +
CC phosphate; Xref=Rhea:RHEA:16169, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000777,
CC ECO:0000256|RuleBase:RU004356};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SUBUNIT: Homooctamer and homotetramer. {ECO:0000256|ARBA:ARBA00038740}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|ARBA:ARBA00009897, ECO:0000256|PROSITE-ProRule:PRU01330,
CC ECO:0000256|RuleBase:RU000384}.
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DR EMBL; CP001029; ACB80494.1; -; Genomic_DNA.
DR RefSeq; WP_012454226.1; NC_010725.1.
DR AlphaFoldDB; B1Z988; -.
DR STRING; 441620.Mpop_2332; -.
DR KEGG; mpo:Mpop_2332; -.
DR eggNOG; COG0174; Bacteria.
DR HOGENOM; CLU_036762_1_0_5; -.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000007136; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:UniProtKB-EC.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR Gene3D; 3.10.20.70; Glutamine synthetase, N-terminal domain; 1.
DR Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR InterPro; IPR008147; Gln_synt_N.
DR InterPro; IPR036651; Gln_synt_N_sf.
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; IPR027302; Gln_synth_N_conserv_site.
DR PANTHER; PTHR20852; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR20852:SF57; GLUTAMINE SYNTHETASE 2 CYTOPLASMIC; 1.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; Glutamine synthetase, N-terminal domain; 1.
DR SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR PROSITE; PS00180; GLNA_1; 1.
DR PROSITE; PS00181; GLNA_ATP; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004356};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU004356};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004356}.
FT DOMAIN 4..86
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 89..348
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 348 AA; 38940 MW; 4AC1EF8323F11FCA CRC64;
MTKFKLEYIW LDGYTPTPNL RGKTQIKEYD SFPTFEQLPL WGFDGSSTQQ AEGSSSDCVL
KPVRHFPDPA RTNGVLVLCE VMMPDGKTPH PSNKRATVLD DAGAWFGFEQ EYFLYKNGRP
LGFPETGYPA PQGPYYCGVG ASNAGPVARK IVEEHLDLCL AAGINHEGIN AEVAKGQWEF
QIFGKGSKKA ADEMWMARYL LQRLCETYEI DIEYHCKPLG DTDWNGSGMH CNFSTTFMRE
TGGKEYFEAM MAQFEKNLDD HIAVYGPDNH MRLTGKHETA PWNKFSYGVA DRGASVRVPH
SFVNNGYKGY LEDRRPNSMG DPYQIASQVL KTISEVPLPA EAAQKAVA
//
