ID A0A2R6W2N0_MARPO Unreviewed; 355 AA.
AC A0A2R6W2N0;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=MARPO_0173s0020 {ECO:0000313|EMBL:PTQ28117.1};
OS Marchantia polymorpha (Common liverwort) (Marchantia aquatica).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=3197 {ECO:0000313|EMBL:PTQ28117.1, ECO:0000313|Proteomes:UP000244005};
RN [1] {ECO:0000313|Proteomes:UP000244005}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tak-1 {ECO:0000313|Proteomes:UP000244005};
RX PubMed=28985561; DOI=10.1016/j.cell.2017.09.030;
RA Bowman J.L., Kohchi T., Yamato K.T., Jenkins J., Shu S., Ishizaki K.,
RA Yamaoka S., Nishihama R., Nakamura Y., Berger F., Adam C., Aki S.S.,
RA Althoff F., Araki T., Arteaga-Vazquez M.A., Balasubrmanian S., Barry K.,
RA Bauer D., Boehm C.R., Briginshaw L., Caballero-Perez J., Catarino B.,
RA Chen F., Chiyoda S., Chovatia M., Davies K.M., Delmans M., Demura T.,
RA Dierschke T., Dolan L., Dorantes-Acosta A.E., Eklund D.M., Florent S.N.,
RA Flores-Sandoval E., Fujiyama A., Fukuzawa H., Galik B., Grimanelli D.,
RA Grimwood J., Grossniklaus U., Hamada T., Haseloff J., Hetherington A.J.,
RA Higo A., Hirakawa Y., Hundley H.N., Ikeda Y., Inoue K., Inoue S.I.,
RA Ishida S., Jia Q., Kakita M., Kanazawa T., Kawai Y., Kawashima T.,
RA Kennedy M., Kinose K., Kinoshita T., Kohara Y., Koide E., Komatsu K.,
RA Kopischke S., Kubo M., Kyozuka J., Lagercrantz U., Lin S.S., Lindquist E.,
RA Lipzen A.M., Lu C.W., De Luna E., Martienssen R.A., Minamino N.,
RA Mizutani M., Mizutani M., Mochizuki N., Monte I., Mosher R., Nagasaki H.,
RA Nakagami H., Naramoto S., Nishitani K., Ohtani M., Okamoto T., Okumura M.,
RA Phillips J., Pollak B., Reinders A., Rovekamp M., Sano R., Sawa S.,
RA Schmid M.W., Shirakawa M., Solano R., Spunde A., Suetsugu N., Sugano S.,
RA Sugiyama A., Sun R., Suzuki Y., Takenaka M., Takezawa D., Tomogane H.,
RA Tsuzuki M., Ueda T., Umeda M., Ward J.M., Watanabe Y., Yazaki K.,
RA Yokoyama R., Yoshitake Y., Yotsui I., Zachgo S., Schmutz J.;
RT "Insights into land plant evolution garnered from the Marchantia polymorpha
RT genome.";
RL Cell 171:287-304.e15(2017).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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; KZ772843; PTQ28117.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R6W2N0; -.
DR EnsemblPlants; PTQ28117; PTQ28117; MARPO_0173s0020.
DR Gramene; PTQ28117; PTQ28117; MARPO_0173s0020.
DR OMA; CHKEHIA; -.
DR Proteomes; UP000244005; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamine synthetase activity; IBA:GO_Central.
DR GO; GO:0006542; P:glutamine biosynthetic process; IBA:GO_Central.
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:SF93; GLUTAMINE SYNTHETASE CYTOSOLIC ISOZYME 1-4; 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:UP000244005}.
FT DOMAIN 19..99
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 106..355
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
FT REGION 40..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 355 AA; 38929 MW; 48D795845238F6C8 CRC64;
MSDLQELVNM KIEDVTSSII AEYIWIGGSG VDIRSKARTL PGPVTSPQEL PKWNYDGSST
GQAPGKDSEV ILYPQAIFRD PFRRGNNILV VCDCYTPAGV PIPTNKRAAA AAIFSKPEVV
KEEPWYGLEQ EYTLLQKEVK WPLGWPVGGY PGPQGPYYCG TGADKAWGRD IVDAHYKACL
YAGIQIGGIN GEVMPGQWEF QVGPSVGIAA GDQLWAARYI LERITEIAGV VLSLDPKPIE
GDWNGAGCHT NFSTKSMRAP GGYKLIKEAI EKLGKRHKEH IAAYGEGNER RLTGKHETAN
MNTFSWGVAN RGSSIRVGRD TEKDGKGYFE DRRPASNMDP YIVTGMIAET TIVMK
//
