ID A0A099XPN0_9FLAO Unreviewed; 337 AA.
AC A0A099XPN0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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 ORFNames=PHEL85_2938 {ECO:0000313|EMBL:KGL58673.1};
OS Polaribacter sp. Hel1_85.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1250005 {ECO:0000313|EMBL:KGL58673.1, ECO:0000313|Proteomes:UP000029991};
RN [1] {ECO:0000313|EMBL:KGL58673.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel1_85 {ECO:0000313|EMBL:KGL58673.1};
RA Xing P., Hahnke R.L., Unfried F., Markert S., Huang S., Barbeyron T.,
RA Harder J., Becher D., Schweder T., Gloenk F.O., Amann R.I., Teeling H.;
RT "Niches of two polysaccharide-degrading Polaribacter strains isolated from
RT the North Sea during a spring diatom bloom.";
RL ISME J. 0:0-0(2014).
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 -!- 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}.
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:KGL58673.1}.
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DR EMBL; JPDS01000003; KGL58673.1; -; Genomic_DNA.
DR RefSeq; WP_036826804.1; NZ_JPDS01000003.1.
DR AlphaFoldDB; A0A099XPN0; -.
DR STRING; 1250005.PHEL85_2938; -.
DR eggNOG; COG0174; Bacteria.
DR OrthoDB; 9807095at2; -.
DR Proteomes; UP000029991; Unassembled WGS sequence.
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 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004356}.
FT DOMAIN 4..87
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 89..337
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 337 AA; 38132 MW; DCBC4431F189BA51 CRC64;
MAKIKLEYIW LDGYKPTQNL RSKTKVEEHE NFQGTIEELG DWSFDGSSTK QAEGGSSDCL
LKPVAIYPDP ARINGYLVMT EVYNADGTPH ESNGRATIDD DDNDFWFGFE QEYFLMDSRT
QLPLGFPIGG YPGPQGMYYC SVGGKNTWGR ELVEEHANLC IDAGLNFEGI NQEVAAGQWE
FQLFAKGAKK AGDEIWIARY LLDRLTEKHH YYIEYHPKPV KGDWNGSGMH ANFSNTILRE
CGSKDKYAEI CEAFRPVTKE HIEVYGEYND ERLTGLHETA SINDFSWGVS DRGASIRIPI
IAVEKGYKGW LEDRRPASNA DPYKIAARII KTVKPVK
//
