GLNA_PANAR
ID GLNA_PANAR Reviewed; 361 AA.
AC Q04831;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Glutamine synthetase {ECO:0000303|PubMed:8100791};
DE EC=6.3.1.2 {ECO:0000250|UniProtKB:P15104};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000305};
OS Panulirus argus (Caribbean spiny lobster) (Palinurus argus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Pleocyemata; Achelata;
OC Palinuroidea; Palinuridae; Panulirus.
OX NCBI_TaxID=6737;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Olfactory organ;
RX PubMed=8100791; DOI=10.1016/0378-1119(93)90279-c;
RA Trapido-Rosenthal H.G., Linser P.J., Greenberg R.M., Gleeson R.A.,
RA Carr W.E.;
RT "cDNA clones from the olfactory organ of the spiny lobster encode a protein
RT related to eukaryotic glutamine synthetase.";
RL Gene 129:275-278(1993).
CC -!- FUNCTION: Glutamine synthetase that catalyzes the ATP-dependent
CC conversion of glutamate and ammonia to glutamine.
CC {ECO:0000250|UniProtKB:P15104}.
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:0000250|UniProtKB:P15104};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P09606};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P15104};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P15104}. Microsome
CC {ECO:0000250|UniProtKB:P09606}. Mitochondrion
CC {ECO:0000250|UniProtKB:P09606}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; M96798; AAA02583.1; -; mRNA.
DR PIR; JN0716; JN0716.
DR AlphaFoldDB; Q04831; -.
DR SMR; Q04831; -.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.10.20.70; -; 1.
DR InterPro; IPR008147; Gln_synt_b-grasp.
DR InterPro; IPR036651; Gln_synt_N.
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 Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; SSF54368; 1.
DR SUPFAM; SSF55931; SSF55931; 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; Cytoplasm; Endoplasmic reticulum; Ligase; Magnesium;
KW Manganese; Metal-binding; Microsome; Mitochondrion; Nucleotide-binding.
FT CHAIN 1..361
FT /note="Glutamine synthetase"
FT /id="PRO_0000153145"
FT DOMAIN 23..103
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 110..361
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
FT BINDING 131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 131
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 133
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 200..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 243..244
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 250
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 252..254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 316
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
FT BINDING 321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 333..335
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 335
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P15104"
FT BINDING 337
FT /ligand="L-glutamate"
FT /ligand_id="ChEBI:CHEBI:29985"
FT /evidence="ECO:0000250|UniProtKB:P9WN39"
SQ SEQUENCE 361 AA; 40768 MW; 3D8C3C507676099C CRC64;
MNQGANKTVL DRYLRLDIPD QKCQAMYIWV DGTGENLRSK TRTLNFTPKS PSELPIWNFD
GSSTGQAERS NSDVYLYPVA VYRDPFRLGN NKLVLCETYK YNKKPADTNQ RWKCMEVMTR
AADQHPWFGM EQEYTLLDID KHPLGWPKNG YPGPQGPYYC GVGANRVYGR DVVEAHYRAC
LCAGINISGE NAKVMPAQWE FQVGPCEGIT MGDDLWMARY LLHRVAEDFD VVVTLDPKPI
PGDWNGAGMH TNFSTEAMRG PNGILEIESA IDKLSKVHEK HIKAYDPHAG KDNERRLTGH
YETSSIHDFS AGVANRGASI RIPRGVAEEK TGYLEDRRPS SNADPYVVSE RLVRTICLNE
Q
