ID G7JN26_MEDTR Unreviewed; 252 AA.
AC G7JN26;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
GN Name=11409211 {ECO:0000313|EnsemblPlants:AES86852};
GN OrderedLocusNames=MTR_4g015590 {ECO:0000313|EMBL:AES86852.1};
GN ORFNames=MtrunA17_Chr4g0006191 {ECO:0000313|EMBL:RHN58792.1};
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:AES86852.1, ECO:0000313|Proteomes:UP000002051};
RN [1] {ECO:0000313|EMBL:AES86852.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:AES86852.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:AES86852,
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 [2] {ECO:0000313|EMBL:AFK48960.1}
RP NUCLEOTIDE SEQUENCE.
RA Krishnakumar V., Cheung F., Xiao Y., Chan A., Moskal W.A., Town C.D.;
RL Submitted (MAY-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AES86852.1, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES86852,
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 [4] {ECO:0000313|EnsemblPlants:AES86852}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES86852};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
RN [5] {ECO:0000313|EMBL:RHN58792.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:RHN58792.1};
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=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001062};
CC -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family.
CC {ECO:0000256|ARBA:ARBA00008345}.
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DR EMBL; CM001220; AES86852.1; -; Genomic_DNA.
DR EMBL; BT149166; AFK48960.1; -; mRNA.
DR EMBL; PSQE01000004; RHN58792.1; -; Genomic_DNA.
DR RefSeq; XP_003604655.1; XM_003604607.2.
DR AlphaFoldDB; G7JN26; -.
DR STRING; 3880.G7JN26; -.
DR MEROPS; C26.A32; -.
DR PaxDb; 3880-AES86852; -.
DR EnsemblPlants; AES86852; AES86852; MTR_4g015590.
DR GeneID; 11409211; -.
DR Gramene; AES86852; AES86852; MTR_4g015590.
DR KEGG; mtr:11409211; -.
DR eggNOG; KOG3210; Eukaryota.
DR HOGENOM; CLU_069674_0_0_1; -.
DR OMA; ENIEMYS; -.
DR OrthoDB; 842at2759; -.
DR Proteomes; UP000002051; Chromosome 4.
DR Proteomes; UP000265566; Chromosome 4.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1903600; C:glutaminase complex; IBA:GO_Central.
DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:EnsemblPlants.
DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IBA:GO_Central.
DR GO; GO:0008614; P:pyridoxine metabolic process; IBA:GO_Central.
DR CDD; cd01749; GATase1_PB; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR HAMAP; MF_01615; PdxT; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR002161; PdxT/SNO.
DR InterPro; IPR021196; PdxT/SNO_CS.
DR NCBIfam; TIGR03800; PLP_synth_Pdx2; 1.
DR PANTHER; PTHR31559; PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO; 1.
DR PANTHER; PTHR31559:SF0; PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO1-RELATED; 1.
DR Pfam; PF01174; SNO; 1.
DR PIRSF; PIRSF005639; Glut_amidoT_SNO; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR PROSITE; PS51273; GATASE_TYPE_1; 1.
DR PROSITE; PS01236; PDXT_SNO_1; 1.
DR PROSITE; PS51130; PDXT_SNO_2; 1.
PE 2: Evidence at transcript level;
KW Glutamine amidotransferase {ECO:0000256|PROSITE-ProRule:PRU00605};
KW Lyase {ECO:0000313|EMBL:RHN58792.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051}.
FT ACT_SITE 79
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005639-1,
FT ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 203
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR005639-1"
FT ACT_SITE 205
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00605"
FT ACT_SITE 205
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR005639-1"
FT BINDING 47..49
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|PIRSR:PIRSR005639-2"
FT BINDING 109
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|PIRSR:PIRSR005639-2"
FT BINDING 143..144
FT /ligand="L-glutamine"
FT /ligand_id="ChEBI:CHEBI:58359"
FT /evidence="ECO:0000256|PIRSR:PIRSR005639-2"
SQ SEQUENCE 252 AA; 27286 MW; 12C883E07287FE69 CRC64;
MAVVGVLALQ GSFNEHIAVL RRLGVKGVEI RKPEQLLTIN SLIIPGGEST TMAKLAQYFN
LFPALREFVQ MGKPVWGTCA GLIFLADKAT GQKTGGQELV GGLDCTVHRN FFGSQIQSFE
TELAVPELVS KEGGPETFRG VFIRAPAILD VGPEVQVLAD YPVPSDKKLS SDSSVEDKKE
NADEKSKVIV AVRQGNILAT AFHPELTADT RWHSYFLKMG NVTGEEASSS VVPAEVSTNN
KLQSQNDLPI FQ
//
