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Database: UniProt
Entry: A0A3Q2G7U8_CYPVA
LinkDB: A0A3Q2G7U8_CYPVA
Original site: A0A3Q2G7U8_CYPVA 
ID   A0A3Q2G7U8_CYPVA        Unreviewed;       371 AA.
AC   A0A3Q2G7U8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 25.
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};
OS   Cyprinodon variegatus (Sheepshead minnow).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC   Cyprinodon.
OX   NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000019800.1, ECO:0000313|Proteomes:UP000265020};
RN   [1] {ECO:0000313|Ensembl:ENSCVAP00000019800.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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   RefSeq; XP_015228079.1; XM_015372593.1.
DR   AlphaFoldDB; A0A3Q2G7U8; -.
DR   STRING; 28743.ENSCVAP00000019800; -.
DR   Ensembl; ENSCVAT00000029044.1; ENSCVAP00000019800.1; ENSCVAG00000023207.1.
DR   GeneID; 107083392; -.
DR   KEGG; cvg:107083392; -.
DR   CTD; 100000775; -.
DR   GeneTree; ENSGT00390000010047; -.
DR   OMA; DRRPNAN; -.
DR   OrthoDB; 1115057at2759; -.
DR   Proteomes; UP000265020; Unplaced.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:SF45; GLUTAMINE SYNTHETASE; 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   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004356};
KW   Reference proteome {ECO:0000313|Proteomes:UP000265020}.
FT   DOMAIN          26..106
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS51986"
FT   DOMAIN          113..371
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   371 AA;  41469 MW;  4E8B05BFFB0B0520 CRC64;
     MATSASASLS KTIKQQYMEL PQGDKVQAMY IWVDGTGEGL RCKTRTLDFE PKSIEDLPEW
     NFDGSSTYQA EGSNSDMYLI PAAMFRDPFR KDPNKLVLCE VQKYNRKPAE TNLRITCKKV
     MDMVADQHPW FGMEQEYTIL GTDGHPFGWP SNGFPGPQGP YYCGVGADKA YGRDIVEAHY
     RACLYAGVNI GGTNAEVMPA QWEFQIGPCE GIDMGDHLWA ARFILHRVCE DFGVVASFDP
     KPIPGNWNGA GCHTNFSTKE MREDGGLKVI EDAIEKLGKR HEYHIRAYDP KGGLDNARRL
     TGRHETSNIH EFSAGVANRG ASIRIPRSVG QEKKGYFEDR RPSANCDPYG VTEALIRTCL
     LNEEGEEPAD Y
//
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