ID E1ANG4_MEDTR Unreviewed; 428 AA.
AC E1ANG4;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=glutamine synthetase {ECO:0000256|ARBA:ARBA00012937};
DE EC=6.3.1.2 {ECO:0000256|ARBA:ARBA00012937};
DE AltName: Full=Glutamate--ammonia ligase {ECO:0000256|ARBA:ARBA00030668};
GN Name=25486062 {ECO:0000313|EnsemblPlants:KEH36738};
GN OrderedLocusNames=MTR_2g021242 {ECO:0000313|EMBL:KEH36738.1};
GN ORFNames=MtrunA17_Chr2g0287181 {ECO:0000313|EMBL:RHN72393.1};
OS Medicago truncatula (Barrel medic) (Medicago tribuloides).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX NCBI_TaxID=3880 {ECO:0000313|EMBL:ADM45299.1};
RN [1] {ECO:0000313|EMBL:ADM45299.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20723225; DOI=10.1186/1471-2229-10-183;
RA Seabra A.R., Vieira C.P., Cullimore J.V., Carvalho H.G.;
RT "Medicago truncatula contains a second gene encoding a plastid located
RT glutamine synthetase exclusively expressed in developing seeds.";
RL BMC Plant Biol. 10:183-183(2010).
RN [2] {ECO:0000313|EMBL:ADM45299.1}
RP NUCLEOTIDE SEQUENCE.
RA Seabra A., Vieira C., Cullimore J., Carvalho H.;
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:KEH36738.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:KEH36738.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH36738,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=22089132; DOI=10.1038/nature10625;
RA Young N.D., Debelle F., Oldroyd G.E., Geurts R., Cannon S.B., Udvardi M.K.,
RA Benedito V.A., Mayer K.F., Gouzy J., Schoof H., Van de Peer Y., Proost S.,
RA Cook D.R., Meyers B.C., Spannagl M., Cheung F., De Mita S.,
RA Krishnakumar V., Gundlach H., Zhou S., Mudge J., Bharti A.K., Murray J.D.,
RA Naoumkina M.A., Rosen B., Silverstein K.A., Tang H., Rombauts S.,
RA Zhao P.X., Zhou P., Barbe V., Bardou P., Bechner M., Bellec A., Berger A.,
RA Berges H., Bidwell S., Bisseling T., Choisne N., Couloux A., Denny R.,
RA Deshpande S., Dai X., Doyle J.J., Dudez A.M., Farmer A.D., Fouteau S.,
RA Franken C., Gibelin C., Gish J., Goldstein S., Gonzalez A.J., Green P.J.,
RA Hallab A., Hartog M., Hua A., Humphray S.J., Jeong D.H., Jing Y.,
RA Jocker A., Kenton S.M., Kim D.J., Klee K., Lai H., Lang C., Lin S.,
RA Macmil S.L., Magdelenat G., Matthews L., McCorrison J., Monaghan E.L.,
RA Mun J.H., Najar F.Z., Nicholson C., Noirot C., O'Bleness M., Paule C.R.,
RA Poulain J., Prion F., Qin B., Qu C., Retzel E.F., Riddle C., Sallet E.,
RA Samain S., Samson N., Sanders I., Saurat O., Scarpelli C., Schiex T.,
RA Segurens B., Severin A.J., Sherrier D.J., Shi R., Sims S., Singer S.R.,
RA Sinharoy S., Sterck L., Viollet A., Wang B.B., Wang K., Wang M., Wang X.,
RA Warfsmann J., Weissenbach J., White D.D., White J.D., Wiley G.B.,
RA Wincker P., Xing Y., Yang L., Yao Z., Ying F., Zhai J., Zhou L., Zuber A.,
RA Denarie J., Dixon R.A., May G.D., Schwartz D.C., Rogers J., Quetier F.,
RA Town C.D., Roe B.A.;
RT "The Medicago genome provides insight into the evolution of rhizobial
RT symbioses.";
RL Nature 480:520-524(2011).
RN [4] {ECO:0000313|EMBL:KEH36738.1, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=A17 {ECO:0000313|EMBL:KEH36738.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:KEH36738,
RC ECO:0000313|Proteomes:UP000002051};
RX PubMed=24767513; DOI=10.1186/1471-2164-15-312;
RA Tang H., Krishnakumar V., Bidwell S., Rosen B., Chan A., Zhou S.,
RA Gentzbittel L., Childs K.L., Yandell M., Gundlach H., Mayer K.F.,
RA Schwartz D.C., Town C.D.;
RT "An improved genome release (version Mt4.0) for the model legume Medicago
RT truncatula.";
RL BMC Genomics 15:312-312(2014).
RN [5] {ECO:0000313|EnsemblPlants:KEH36738}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:KEH36738};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
RN [6] {ECO:0000313|Proteomes:UP000265566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Jemalong A17 {ECO:0000313|Proteomes:UP000265566};
RX PubMed=30397259; DOI=10.1038/s41477-018-0286-7;
RA Pecrix Y., Staton S.E., Sallet E., Lelandais-Briere C., Moreau S.,
RA Carrere S., Blein T., Jardinaud M.F., Latrasse D., Zouine M., Zahm M.,
RA Kreplak J., Mayjonade B., Satge C., Perez M., Cauet S., Marande W.,
RA Chantry-Darmon C., Lopez-Roques C., Bouchez O., Berard A., Debelle F.,
RA Munos S., Bendahmane A., Berges H., Niebel A., Buitink J., Frugier F.,
RA Benhamed M., Crespi M., Gouzy J., Gamas P.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 4:1017-1025(2018).
RN [7] {ECO:0000313|EMBL:RHN72393.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:RHN72393.1};
RA Pecrix Y., Gamas P., Carrere S.;
RT "Whole-genome landscape of Medicago truncatula symbiotic genes.";
RL Nat. Plants 0:0-0(2018).
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 -!- SUBUNIT: Homooctamer. {ECO:0000256|ARBA:ARBA00011823}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229}.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
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DR EMBL; HM775420; ADM45299.1; -; mRNA.
DR EMBL; HM775421; ADM45300.1; -; mRNA.
DR EMBL; CM001218; KEH36738.1; -; Genomic_DNA.
DR EMBL; PSQE01000002; RHN72393.1; -; Genomic_DNA.
DR RefSeq; XP_013462703.1; XM_013607249.1.
DR AlphaFoldDB; E1ANG4; -.
DR STRING; 3880.E1ANG4; -.
DR EnsemblPlants; KEH36738; KEH36738; MTR_2g021242.
DR GeneID; 120575736; -.
DR Gramene; KEH36738; KEH36738; MTR_2g021242.
DR KEGG; mtr:120575736; -.
DR eggNOG; KOG0683; Eukaryota.
DR eggNOG; KOG1075; Eukaryota.
DR HOGENOM; CLU_036762_1_1_1; -.
DR OrthoDB; 1115057at2759; -.
DR Proteomes; UP000002051; Chromosome 2.
DR Proteomes; UP000265566; Chromosome 2.
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 PANTHER; PTHR20852; GLUTAMINE SYNTHETASE; 1.
DR PANTHER; PTHR20852:SF117; GLUTAMINE SYNTHETASE, CHLOROPLASTIC_MITOCHONDRIAL; 1.
DR Pfam; PF00120; Gln-synt_C; 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; 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};
KW Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ADM45299.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Plastid {ECO:0000256|ARBA:ARBA00022640};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 75..155
FT /note="GS beta-grasp"
FT /evidence="ECO:0000259|PROSITE:PS51986"
FT DOMAIN 159..428
FT /note="GS catalytic"
FT /evidence="ECO:0000259|PROSITE:PS51987"
SQ SEQUENCE 428 AA; 47212 MW; 71F23C915E6EBDB4 CRC64;
MAQILAPSTQ CQTRITKTSP FATPISSKMW SSLVMKQNKK VARSATFRAM AINSGTINRV
EDLLNLDITP FTDSIIAEYI WIGGTGIDVR SKSRTISKPV EHPSELPKWN YDGSSTGQAP
GEDTEVILYP QAIFKDPFRG GNNILVICDA YTTQGEPIPT NKRYKAAQIF RNPKVEAEIP
WFGIEQEYTL LQTNVKWPLG WPVGGYPGPQ GPYYCGAGAD KSFGRDISDA HYKACLYAGI
NISGTNAEVM PGQWEYQVGP SVGTEAADHI WASRYILERI TEQAGVVLSL DPKPIEGDWN
GAGCHTNYST KSMREDGGFE VIKKAILNLS LRHKVHMEAY GEGNERRLTG KHETASIDTF
SWGIGKRGCS IRVGRETEKN GKGYLEDRRP ASNMDPYVVT ALLAESTLLW EPTLEAEALA
AQKLALKV
//
