ID A0A4U8Z3Q6_METTU Unreviewed; 347 AA.
AC A0A4U8Z3Q6;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:VFU09971.1};
DE EC=6.3.1.2 {ECO:0000313|EMBL:VFU09971.1};
GN ORFNames=MTUNDRAET4_3084 {ECO:0000313|EMBL:VFU09971.1};
OS Methylocella tundrae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Methylocella.
OX NCBI_TaxID=227605 {ECO:0000313|EMBL:VFU09971.1, ECO:0000313|Proteomes:UP000294360};
RN [1] {ECO:0000313|EMBL:VFU09971.1, ECO:0000313|Proteomes:UP000294360}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MTUNDRAET4 annotated genome {ECO:0000313|EMBL:VFU09971.1};
RA Kox A.R. M.;
RL Submitted (MAR-2019) 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
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DR EMBL; LR536450; VFU09971.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4U8Z3Q6; -.
DR KEGG; mtun:MTUNDRAET4_3084; -.
DR Proteomes; UP000294360; Chromosome 1.
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 PANTHER; PTHR43785; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE; 1.
DR PANTHER; PTHR43785:SF12; GAMMA-GLUTAMYLPUTRESCINE SYNTHETASE PUUA; 1.
DR Pfam; PF00120; Gln-synt_C; 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; PS00181; GLNA_ATP; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:VFU09971.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Reference proteome {ECO:0000313|Proteomes:UP000294360}.
FT DOMAIN 12..94
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 100..347
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT REGION 289..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 347 AA; 39268 MW; 13485909BDD6E5B9 CRC64;
MSTLLSEVAA ERGIKNFLVS YTDLFGHMRA KLVPARAIDK MARDGAGFAG FATWLDMTPA
MPDMFAVPDP DSLIQLPWKR EVGWLAADLY MEGKPVDQGP RNVLKRLIAE LKELGYEMRA
GVECEFFLLA PDGSCIADGA DKQAKSCYDQ QALMRRYEVI TEISEAMDEL GWKPYQSDHE
DANGQFEMNW EYDEALKTAD RHSFFKYMVK SLAEKHGMRA TFMPKPFLNL TGSGCHSHVS
LWRGEDNAFE DKDGELGVSE LGYRFLGGLM EHADALCALT NPTVNSYKRL SAPRTTSGAT
RAELDHLHRQ QQDAYDPHSR RRTLRVPPRR RRDESLSAAG QRPRRRP
//
