ID A0A2K4GFQ5_9PSED Unreviewed; 458 AA.
AC A0A2K4GFQ5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Glutamine synthetase {ECO:0000313|EMBL:POA22387.1};
GN ORFNames=C1886_01775 {ECO:0000313|EMBL:POA22387.1};
OS Pseudomonas sp. FW300-N1A1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=2075555 {ECO:0000313|EMBL:POA22387.1, ECO:0000313|Proteomes:UP000236411};
RN [1] {ECO:0000313|EMBL:POA22387.1, ECO:0000313|Proteomes:UP000236411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FW300-N1A1 {ECO:0000313|EMBL:POA22387.1,
RC ECO:0000313|Proteomes:UP000236411};
RA Spencer S.J., Aaring A.B., Hendricks A., Penterman J., Chakraborty R.,
RA Alm E.J.;
RT "Whole genome sequencing of deep branching strains shows evolution and
RT exchange across a contaminated watershed.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
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:POA22387.1}.
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DR EMBL; PPSF01000002; POA22387.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K4GFQ5; -.
DR Proteomes; UP000236411; Unassembled WGS sequence.
DR GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
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 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 Magnesium {ECO:0000256|ARBA:ARBA00022842}.
FT DOMAIN 21..116
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 123..458
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 458 AA; 51017 MW; 0A1C5D4749BE2002 CRC64;
MSVPPRAVQL NEANAFLKEH PEVLYVDLLI ADMNGVVRGK RIERTSLHKV YEKGINLPAS
LFALDINGST VESTGLGLDI GDADRICYPI PDTLCNEPWQ KRPTAQLLMT MHELEGEPFF
ADPREVLANV VRKFDEMGLT ICAAFELEFY LIDQENVNGR PQPPRSPVSG KRPHSTQVYL
IDDLDEYVDC LQDILEGAKE QGIPADAIVK ESAPAQFEVN LHHVADPIKA CDYAVLLKRL
IKNIAYDHEM DTTFMAKPYP GQAGNGLHVH ISILDKDGKN IFASEDPEQN AALRHAIGGV
LETLPAQMAF LCPNVNSYRR FGAQFYVPNS PCWGLDNRTV AIRVPTGSSD AVRIEHRVAG
ADANPYLLMA SVLAGVHHGL VNKIEPGAPV EGNSYEQNEQ SLPNNLRDAL RELDDSEVMA
KYIDPKYIDI FVACKESELE EFEHSISDLE YNWYLHTV
//
