ID A0A3S3NU33_9ACAR Unreviewed; 358 AA.
AC A0A3S3NU33;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=glutamine synthetase {ECO:0000256|ARBA:ARBA00012937};
DE EC=6.3.1.2 {ECO:0000256|ARBA:ARBA00012937};
GN ORFNames=B4U79_12645 {ECO:0000313|EMBL:RWR98652.1};
OS Dinothrombium tinctorium.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Trombidiformes; Prostigmata; Anystina; Parasitengona;
OC Trombidioidea; Trombidiidae; Dinothrombium.
OX NCBI_TaxID=1965070 {ECO:0000313|EMBL:RWR98652.1, ECO:0000313|Proteomes:UP000285301};
RN [1] {ECO:0000313|EMBL:RWR98652.1, ECO:0000313|Proteomes:UP000285301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UoL-WK {ECO:0000313|EMBL:RWR98652.1};
RA Dong X., Chaisiri K., Xia D., Armstrong S.D., Fang Y., Donnelly M.J.,
RA Kadowaki T., McGarry J.W., Darby A.C., Makepeace B.L.;
RT "Genomes of trombidid mites reveal novel predicted allergens and laterally-
RT transferred genes associated with secondary metabolism.";
RL Gigascience 0:0-0(2018).
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|ARBA:ARBA00000777};
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RWR98652.1}.
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DR EMBL; NCKU01019997; RWR98652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S3NU33; -.
DR STRING; 1965070.A0A3S3NU33; -.
DR Proteomes; UP000285301; Unassembled WGS sequence.
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; 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 PANTHER; PTHR20852; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR20852:SF57; GLUTAMINE SYNTHETASE 2 CYTOPLASMIC; 1.
DR Pfam; PF00120; Gln-synt_C; 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; 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};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000285301}.
FT DOMAIN 20..100
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 107..358
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 358 AA; 39933 MW; 1235A4EEBBC307B4 CRC64;
MSNKFVLEKY LSLRQPTDKI QVNYVWIDGT GGCLRSKTRT LGFIPRQASD LPKWRYCGSA
TGQATGNKAE YSLKPVALYN DPFRRGNNKI VLCDTYDVSD SPTLTNKRNS CAASLAKLSQ
QYDPWFGIEQ EYTLLDSSDG RPLGWPKNGF PGPQGPYYCG VGAGKVYGRD VIESHYRACL
YAGIPLAGEN AEVMPAQWEF QVGPCEGITM GDDLWMARFI LHRVAEEFDV CVSFDPKPIA
GDWNGAGAHC NFSTKQMREK DGIKHIEEAI EKLRCNHQEH IKLYDPKGGE DNARRLTGKH
ETSQINIFTC GVGDRGASVR IPRQVAEDGF GYLEDRRPAS NCDPYVVIEA LVKTVLLE
//
