GLNA1_DAUCA
ID GLNA1_DAUCA Reviewed; 352 AA.
AC O22504;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Glutamine synthetase cytosolic isozyme;
DE EC=6.3.1.2;
DE AltName: Full=GS1;
DE AltName: Full=Glutamate--ammonia ligase;
GN Name=GLN1;
OS Daucus carota (Wild carrot).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC Daucus; Daucus sect. Daucus.
OX NCBI_TaxID=4039;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. US-Harumakigosun;
RA Higashi K., Kamada H.;
RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Homooctamer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family. {ECO:0000305}.
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DR EMBL; AF019559; AAB71691.1; -; mRNA.
DR PIR; T14290; T14290.
DR AlphaFoldDB; O22504; -.
DR SMR; O22504; -.
DR GO; GO:0005737; C:cytoplasm; 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: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; Ligase; Nucleotide-binding.
FT CHAIN 1..352
FT /note="Glutamine synthetase cytosolic isozyme"
FT /id="PRO_0000153170"
FT DOMAIN 19..98
FT /note="GS beta-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01330"
FT DOMAIN 105..352
FT /note="GS catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01331"
SQ SEQUENCE 352 AA; 38340 MW; D12BE42E4F56E0A5 CRC64;
MASLTDLINL DLSDTTDKFI AEYIWIDAVG GLRSKARTLS GPVDDPTKLP KWNFDGSSTG
QGPGDDSEVI IYPQAIFKDP FRRGNHILVM CDTYTPAGEP IPTNKRCNAA KIFSHPDVAA
EVPWFGIEQE YTLLKKEVNC PIGCPTGGYP GPQGPYYCGI GADKAFGRDI VDAHYKACLY
AGINISGING EVMPGQWEFQ VGPAVGISAG DELWVARYIL ERITEIAGVV VSLDPKPIPG
DWNGAGAHTN YSTKSMRNEG GFEIIKKAIA KLETKHAQHI AAYGEGNERR LTGKHETASI
HKFSWGVANR GASVRVGRDT EKEGKGYFED RRPASNMEPY VVTSMIAETT IL