ID Q7SZ38_XENLA Unreviewed; 373 AA.
AC Q7SZ38;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 99.
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 Name=glull.1.S {ECO:0000313|Xenbase:XB-GENE-990058};
GN Synonyms=glul {ECO:0000313|RefSeq:NP_001080899.1}, glul-like
GN {ECO:0000313|Xenbase:XB-GENE-990058}, glul-like.1
GN {ECO:0000313|Xenbase:XB-GENE-990058}, glul-like.1.S
GN {ECO:0000313|RefSeq:NP_001080899.1,
GN ECO:0000313|Xenbase:XB-GENE-990058}, gso2
GN {ECO:0000313|RefSeq:NP_001080899.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH54153.1};
RN [1] {ECO:0000313|RefSeq:NP_001080899.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|RefSeq:NP_001080899.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12654890; DOI=10.1242/jeb.00283;
RA Murray B.W., Busby E.R., Mommsen T.P., Wright P.A.;
RT "Evolution of glutamine synthetase in vertebrates: multiple glutamine
RT synthetase genes expressed in rainbow trout (Oncorhynchus mykiss).";
RL J. Exp. Biol. 206:1511-1521(2003).
RN [3] {ECO:0000313|EMBL:AAH54153.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Whole {ECO:0000313|EMBL:AAH54153.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|RefSeq:NP_001080899.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) 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|RuleBase:RU004356};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
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; BC054153; AAH54153.1; -; mRNA.
DR RefSeq; NP_001080899.1; NM_001087430.2.
DR STRING; 8355.Q7SZ38; -.
DR PaxDb; 8355-Q7SZ38; -.
DR DNASU; 380593; -.
DR GeneID; 380593; -.
DR KEGG; xla:380593; -.
DR AGR; Xenbase:XB-GENE-990058; -.
DR CTD; 380593; -.
DR Xenbase; XB-GENE-990058; glull.1.S.
DR OMA; DRRPNAN; -.
DR OrthoDB; 1115057at2759; -.
DR Proteomes; UP000186698; Chromosome 4S.
DR Bgee; 380593; Expressed in brain and 19 other cell types or tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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:SF45; 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; PS00181; GLNA_ATP; 1.
DR PROSITE; PS51986; GS_BETA_GRASP; 1.
DR PROSITE; PS51987; GS_CATALYTIC; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004356};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU004356};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004356};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698}.
FT DOMAIN 26..106
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 113..373
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 373 AA; 42088 MW; 881DB61A82C03663 CRC64;
MATSASAQLS KAIKQMYLEL PQGDKVQAMY IWIDGTGEGL RCKTRTLDSE PKTIEDLPEW
NFDGSSTHQS EGSNSDMYLI PVAMFRDPFR RDPNKLVLCE VLKYNRKTAE TNLRHTCNQI
MDMVGNEHPW FGMEQEYTLL GMDGHPFGWP SNGFPGPQGP YYCGVGANKA YGRDIVEAHY
RACLYAGVKI AGTNAEVMPA QWEFQIGTCE GIDMGDHLWI ARFILHRVCE DFGIIVSFDP
KPITGNWNGA GCHTNFSTKS MREEGGLKHI EESIERLSKR HEYHIRMYDP RGGKDNARRL
TGFHETSSIH EFSAGVANRG ASIRIPRLVG QEKKGYFEDR RPSANCDPYA VTEAVIRTCL
LNETGDEPLE YKN
//
