ID A0A1I3IG77_9ACTN Unreviewed; 492 AA.
AC A0A1I3IG77;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=glutamine synthetase {ECO:0000256|ARBA:ARBA00012937};
DE EC=6.3.1.2 {ECO:0000256|ARBA:ARBA00012937};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000256|ARBA:ARBA00030668};
DE AltName: Full=Glutamine synthetase I beta {ECO:0000256|ARBA:ARBA00033230};
GN ORFNames=SAMN05216561_1094 {ECO:0000313|EMBL:SFI46994.1};
OS Nocardioides psychrotolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1005945 {ECO:0000313|EMBL:SFI46994.1, ECO:0000313|Proteomes:UP000198649};
RN [1] {ECO:0000313|EMBL:SFI46994.1, ECO:0000313|Proteomes:UP000198649}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11156 {ECO:0000313|EMBL:SFI46994.1,
RC ECO:0000313|Proteomes:UP000198649};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; FOQG01000009; SFI46994.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3IG77; -.
DR STRING; 1005945.SAMN05216561_1094; -.
DR OrthoDB; 3277468at2; -.
DR Proteomes; UP000198649; 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 PANTHER; PTHR43407; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR43407:SF1; LENGSIN; 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; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 3: Inferred from homology;
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000198649}.
FT DOMAIN 32..120
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 127..492
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 492 AA; 54014 MW; 0238355F6BE23210 CRC64;
MPIDVFEPHP LVRLLGKPAA DFTCSDLVRA VEQLELRQVN LRYVGGDGRL KTIAFPIGSR
EHLVEVLTRG ERVDGSSIFE GTETEASDVY IVPRHRTAFL NPFGERTSLD VLCSFYSQDG
DPLPYAYEQI VRRAAEVLTQ ETGLVLEAFG ELEYYLVGEV ERIFPVQAER GYQESAPFSK
GQQVREEVLG HLAEMGIKLK YAHGEVGNIL EEERQLVQHE IEFWPVPVEQ AADALVLAKW
VVRQVAYAHG LEVTFAPSVS SDGAGSGLHV HTRLVRDGAS EIVGEDGIND TGRRLIAGYL
SAAKALTAFG NTVPTSYLRF SDGEEAPEGI CWGDTDRTGL VRVPLAWGGH VLPGMVAHAN
PDSSESIPEP AIHPQTIELR LGDGSADVHL LLAGMAVAAR RGLSDPDSLD QAERLNTADH
DDFEQLPTSC AESADALENE RTSFEADGIF PSELIDAVLD RLREADAAAQ MKKVKKDDDA
REELVRRYWH VG
//
