ID A0A131ZX05_SARSC Unreviewed; 398 AA.
AC A0A131ZX05;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
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};
GN ORFNames=QR98_0017670 {ECO:0000313|EMBL:KPM03336.1}, SSS_7883
GN {ECO:0000313|EMBL:KAF7495467.1};
OS Sarcoptes scabiei (Itch mite) (Acarus scabiei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Psoroptidia; Sarcoptoidea;
OC Sarcoptidae; Sarcoptinae; Sarcoptes.
OX NCBI_TaxID=52283 {ECO:0000313|EMBL:KPM03336.1, ECO:0000313|Proteomes:UP000616769};
RN [1] {ECO:0000313|EMBL:KPM03336.1, ECO:0000313|Proteomes:UP000616769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Arlian Lab {ECO:0000313|EMBL:KPM03336.1};
RX PubMed=26555130; DOI=10.1186/s13071-015-1198-2;
RA Rider S.D.Jr., Morgan M.S., Arlian L.G.;
RT "Draft genome of the scabies mite.";
RL Parasit. Vectors 8:585-585(2015).
RN [2] {ECO:0000313|Proteomes:UP000070412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=33001992;
RA Korhonen P.K., Gasser R.B., Ma G., Wang T., Stroehlein A.J., Young N.D.,
RA Ang C.S., Fernando D.D., Lu H.C., Taylor S., Reynolds S.L., Mofiz E.,
RA Najaraj S.H., Gowda H., Madugundu A., Renuse S., Holt D., Pandey A.,
RA Papenfuss A.T., Fischer K.;
RT "High-quality nuclear genome for Sarcoptes scabiei-A critical resource for
RT a neglected parasite.";
RL PLoS Negl. Trop. Dis. 14:0-0(2020).
RN [3] {ECO:0000313|EMBL:KAF7495467.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SSS_KF_BRIS2020 {ECO:0000313|EMBL:KAF7495467.1};
RA Korhonen P.K.K., Guangxu M.G., Wang T.W., Stroehlein A.J.S., Young N.D.,
RA Ang C.-S.A., Fernando D.W.F., Lu H.L., Taylor S.T., Ehtesham M.E.M.,
RA Najaraj S.H.N., Harsha G.H.G., Madugundu A.M., Renuse S.R., Holt D.H.,
RA Pandey A.P., Papenfuss A.P., Gasser R.B.G., Fischer K.F.;
RL Submitted (JAN-2020) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EnsemblMetazoa:KAF7495467.1}
RP IDENTIFICATION.
RG EnsemblMetazoa;
RL Submitted (JUN-2022) 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|ARBA:ARBA00000777,
CC ECO:0000256|RuleBase:RU004356};
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; WVUK01000048; KAF7495467.1; -; Genomic_DNA.
DR EMBL; JXLN01004651; KPM03336.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A131ZX05; -.
DR EnsemblMetazoa; SSS_7883s_mrna; KAF7495467.1; SSS_7883.
DR VEuPathDB; VectorBase:SSCA004897; -.
DR OMA; TKDYADH; -.
DR OrthoDB; 1115057at2759; -.
DR Proteomes; UP000070412; Unassembled WGS sequence.
DR Proteomes; UP000616769; 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; 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:SF57; GLUTAMINE SYNTHETASE 2 CYTOPLASMIC; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004356};
KW Reference proteome {ECO:0000313|Proteomes:UP000070412}.
FT DOMAIN 59..139
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 146..398
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT REGION 320..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 398 AA; 44527 MW; C3DA717436D60CFB CRC64;
MSRIITTRSL WNKLIGGDKL CNNLVKLLKN QNRFVHTRLE SNARILANYT SLKQPENTVI
AEYIWIDGSG ENIRSKARTL LEHPKTVNDL PRWNFDGSST GQSHGSNSDV YLKPVRIYKD
PIRKGDNILV LCETINYDNT PHITNKRHTC VEAMEKAASV DPTFGLEQEY SLLDGNEPNK
MLGWPTGGYP EPQGPYYCGV GAGKAFGRDV IEAHYRACLY ADIAISGVNA EVMASQWEFQ
VGPTIGVRCA DDLWLARYLL HRIAEDFNIK VTFDPKPIQG DWNGAGCHAN FSTNDMIAEG
GLKAIEAAMP KLDKNHLKHI RNYDPKGGQD NTRRLTGKHE TSSMEKFSYG VANRGASVRI
PRSVADKGKG YLEDRRPASN MDPYVVCELL VRTIVLNE
//
