ID E3M878_CAERE Unreviewed; 392 AA.
AC E3M878;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=glutamine synthetase {ECO:0000256|ARBA:ARBA00012937};
DE EC=6.3.1.2 {ECO:0000256|ARBA:ARBA00012937};
GN ORFNames=CRE_13325 {ECO:0000313|EMBL:EFO94423.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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; DS268428; EFO94423.1; -; Genomic_DNA.
DR RefSeq; XP_003107602.1; XM_003107554.1.
DR AlphaFoldDB; E3M878; -.
DR STRING; 31234.E3M878; -.
DR EnsemblMetazoa; CRE13325.1; CRE13325.1; WBGene00061501.
DR eggNOG; KOG0683; Eukaryota.
DR HOGENOM; CLU_036762_1_1_1; -.
DR InParanoid; E3M878; -.
DR OMA; QVWIARF; -.
DR OrthoDB; 1115057at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
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; 2.
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; IPR027302; Gln_synth_N_conserv_site.
DR PANTHER; PTHR20852; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR20852:SF39; 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; PS51986; GS_BETA_GRASP; 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:UP000008281}.
FT DOMAIN 30..114
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 117..392
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 392 AA; 44139 MW; 2B9DDA0D774AD467 CRC64;
MSHLNYETRL PLGQATIDHF MCLPAHPSKC QATYVWIDGT GEQLRAKTRT FDVKPKYVSE
YPVWNYDGSS TGQAEGDNSD RYLRPVAVFP DPFSGGHNVL VMCDTLDNKM KPTVTNHRQA
CAAIMKQVAD QHPWFGMEQE YLIVDRDEHP LGWPKHGYPA PQGKYYCGVG ADRAFGREVV
ETHYRACLHA GINIFGANAE VTPGQWEYQI GTCEGIDMGD QLWISRYILH RVAEMFGVCI
SLDPKPKVTM GDWNGAGCHT NFSTSEMRKP NGLTAIFEAM KADLSKIGPA RFFLRLEKTH
LEAMKVYDPN GGQDNLRRLT GRHETSQADK FSWGVANRAC SIRIPRQVAD EAKGYLEDRR
PPLQGYLEDR RPSSNCDPYL VTAMIVKSVL LD
//
