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Database: UniProt
Entry: A0A3B3DMI4_ORYME
LinkDB: A0A3B3DMI4_ORYME
Original site: A0A3B3DMI4_ORYME 
ID   A0A3B3DMI4_ORYME        Unreviewed;       250 AA.
AC   A0A3B3DMI4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=glutamine synthetase {ECO:0000256|ARBA:ARBA00012937};
DE            EC=6.3.1.2 {ECO:0000256|ARBA:ARBA00012937};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000030575.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000030575.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01331, ECO:0000256|RuleBase:RU000384}.
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DR   AlphaFoldDB; A0A3B3DMI4; -.
DR   Ensembl; ENSOMET00000021048.1; ENSOMEP00000030575.1; ENSOMEG00000015310.1.
DR   GeneTree; ENSGT00940000164772; -.
DR   Proteomes; UP000261560; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 2.
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; PTHR20852; GLUTAMINE SYNTHETASE; 1.
DR   PANTHER; PTHR20852:SF43; GLUTAMINE SYNTHETASE; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          5..250
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   250 AA;  28139 MW;  BE455821C75F079C CRC64;
     MNIWLRCTTT GKITFVFLML TTTFAALRSF YVEQDYFILN ESPYYCGVGA NSAYGRDIVE
     SHYKACLYAG VKICGTNAEV MPSQWEYQVG ICEGIEMGDH LWVSRFLLHR VCEDFGVLAT
     LDPKPVKGNW NGSGCHTNVS TKQMREEGGL LHIEAAIEKL SKHHQEHIRV YDLHNGQDNM
     RRLTGMHETS SIHDFSAGVA NRGASIRIPR QVGKDKKGYF EDRRPASNCD PYMVTAAIAE
     TCLLESEEGE
//
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