ID A0A257JNM4_9PROT Unreviewed; 461 AA.
AC A0A257JNM4;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:OYU76722.1};
GN ORFNames=CFE32_08995 {ECO:0000313|EMBL:OYU76722.1};
OS Alphaproteobacteria bacterium PA3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=2015571 {ECO:0000313|EMBL:OYU76722.1, ECO:0000313|Proteomes:UP000215583};
RN [1] {ECO:0000313|EMBL:OYU76722.1, ECO:0000313|Proteomes:UP000215583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA3 {ECO:0000313|EMBL:OYU76722.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OYU76722.1}.
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DR EMBL; NKIV01000183; OYU76722.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257JNM4; -.
DR Proteomes; UP000215583; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
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:SF3; GLN-SYNT_C DOMAIN-CONTAINING PROTEIN; 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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Reference proteome {ECO:0000313|Proteomes:UP000215583}.
FT DOMAIN 23..120
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 127..461
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 461 AA; 51187 MW; 5CF14D331A53514A CRC64;
MSFETDPSIH KRLEAWIKEK GVSEIELILP DMNGIIRGKV VPAARFLKGV SNHTLRIASS
ILRVTVTGEY PDAESDDEDG FSGTLDPDCV LVPDPASICV APGYRTPTAY VVTDAYTHAG
KLIDIAPRQV LRRVLDLYAE RGWEPVVAPE VEFFLTARNI DPDLPLETPV GRSGRAETVS
QPYGLEAINE YEDLIEQIYE YCEIAELDID TMIHEAGAAQ LEVNFNHGDA LELADQVLMF
KRIVRQVALS QNVYATFMAK PMDNQPGSAM HIHQSLVDKE TGRNLFANTN GTDSKLFRSF
VGGLQTYLPD VAPLFAPNVN SFRRMRPQFD APINVQWGLD NRSCGLRTPI SDGRNRRVEN
RLPGADANSY LAIASSLACG YVGMVQGLEP GPLITTSAYR MPRSLPRTLD EALGRFQNCE
PMREVLGEEF CRVFAAVKLD ELDAFEGVVS AWEREHLLLK V
//
