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Database: UniProt
Entry: A0A5E4ADF6_MARMO
LinkDB: A0A5E4ADF6_MARMO
Original site: A0A5E4ADF6_MARMO 
ID   A0A5E4ADF6_MARMO        Unreviewed;       297 AA.
AC   A0A5E4ADF6;
DT   13-NOV-2019, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=glutamine synthetase {ECO:0000256|ARBA:ARBA00012937};
DE            EC=6.3.1.2 {ECO:0000256|ARBA:ARBA00012937};
GN   ORFNames=GHT09_020172 {ECO:0000313|EMBL:KAF7468883.1}, MONAX_5E027734
GN   {ECO:0000313|EMBL:VTJ55373.1};
OS   Marmota monax (Woodchuck).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC   Xerinae; Marmotini; Marmota.
OX   NCBI_TaxID=9995 {ECO:0000313|EMBL:VTJ55373.1, ECO:0000313|Proteomes:UP000335636};
RN   [1] {ECO:0000313|EMBL:VTJ55373.1, ECO:0000313|Proteomes:UP000335636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Alioto T., Alioto T.;
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KAF7468883.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=WC2-LM {ECO:0000313|EMBL:KAF7468883.1};
RC   TISSUE=Liver {ECO:0000313|EMBL:KAF7468883.1};
RA   Shumante A., Zimin A.V., Puiu D., Salzberg S.L.;
RL   Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01331, ECO:0000256|RuleBase:RU000384}.
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DR   EMBL; WJEC01007707; KAF7468883.1; -; Genomic_DNA.
DR   EMBL; CABDUW010000049; VTJ55373.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A5E4ADF6; -.
DR   Proteomes; UP000335636; Unassembled WGS sequence.
DR   Proteomes; UP000662637; Unassembled WGS sequence.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; 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: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; 2.
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; PTHR20852; GLUTAMINE SYNTHETASE; 1.
DR   PANTHER; PTHR20852:SF45; 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000335636}.
FT   DOMAIN          37..297
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   297 AA;  33667 MW;  2BF2CBCA40F24D85 CRC64;
     MYLVPAAMFR DPFPKDPNKL VFCEVFKYNR KPAETNLRHT CKRIMEMVSN QHPWFGMEQE
     YTLMGTDGHP FGWPSNGFPG PQGPYYCGVG ADKAYGRDIV EAHYRACLYA GVMITGTNAE
     VMPAQWEFQI GPCEGIHMGD HLWVARFILH RVCEDFGVIA TFDPKPIPGN WNGAGCHTNF
     STKAMMEENG LKYIEEAIEK LSKRHQYHIR AYDPKGGLDN ARRLTGFHET SNINDFSAGV
     ANRSASIHIP RTVGQERRGY FEDRRPSANC DPCSVTEALI RTCLLNETGD EPFQYKN
//
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