ID A0A5B8MYW8_9CHLO Unreviewed; 369 AA.
AC A0A5B8MYW8;
DT 13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2019, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=A3770_18p80790 {ECO:0000313|EMBL:QDZ25561.1};
OS Chloropicon primus.
OC Eukaryota; Viridiplantae; Chlorophyta; Chloropicophyceae; Chloropicales;
OC Chloropicaceae; Chloropicon.
OX NCBI_TaxID=1764295 {ECO:0000313|EMBL:QDZ25561.1, ECO:0000313|Proteomes:UP000316726};
RN [1] {ECO:0000313|EMBL:QDZ25561.1, ECO:0000313|Proteomes:UP000316726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCMP1205 {ECO:0000313|EMBL:QDZ25561.1,
RC ECO:0000313|Proteomes:UP000316726};
RA Pombert J.-F., Otis C., Turmel M., Lemieux C.;
RT "The complete nuclear genome of the prasinophyte Chloropicon primus
RT (CCMP1205).";
RL Submitted (JUL-2018) 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|RuleBase:RU004356};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; CP031051; QDZ25561.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5B8MYW8; -.
DR STRING; 1764295.A0A5B8MYW8; -.
DR Proteomes; UP000316726; Chromosome 18.
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:SF93; GLUTAMINE SYNTHETASE CYTOSOLIC ISOZYME 1-4; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000316726}.
FT DOMAIN 34..114
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 121..369
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 369 AA; 40513 MW; DCD7FD424878557D CRC64;
MTKGNGIAME DVKEHTGATS VEELLKMPTP LSSTVVEYIW IDGTMENCRS KARVVTKRVT
SVDQLSKWNF DGSSTGQAGG EDSEVILVPK AIYRDPFRGG QHLLCMCECE DPFGNALKTN
SRRAAAKIFE DPKVKGEEPW YGIEQEYALL DAKTNWPLGW PEQGFPGPQG PYYCAVGANK
ISGREICDAH FKACLYAGLN ISGTNGEVMP SQWEYQIGPC TGIESGDQMW ISRYLLERIC
EMAGVVVSLD PKPIPGDWNG SGAHTNYSTK SMRADGGMAH IKKAIGKLEE KHMEHIKAYG
EGNERRLTGA HETASIDAFS WGVANRGASV RVGRDTERDG KGYMEDRRPA SNMDPYVVTS
LIAKTTILS
//
