ID B7FLG0_MEDTR Unreviewed; 542 AA.
AC B7FLG0;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Glutamyl-tRNA reductase {ECO:0000256|ARBA:ARBA00012970, ECO:0000256|RuleBase:RU000584};
DE EC=1.2.1.70 {ECO:0000256|ARBA:ARBA00012970, ECO:0000256|RuleBase:RU000584};
GN Name=11421100 {ECO:0000313|EnsemblPlants:AES98352};
GN OrderedLocusNames=MTR_5g067410 {ECO:0000313|EMBL:AES98352.1};
GN ORFNames=MtrunA17_Chr5g0428201 {ECO:0000313|EMBL:RHN56320.1};
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:ACJ85594.1};
RN [1] {ECO:0000313|EMBL:ACJ85594.1}
RP NUCLEOTIDE SEQUENCE.
RA Moskal W., Chan A., Cheung F., Xiao Y., Town C.D.;
RT "Medicago truncatula full length cdna cloning project.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AES98352.1, ECO:0000313|Proteomes:UP000002051}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A17 {ECO:0000313|EMBL:AES98352.1}, and cv. Jemalong A17
RC {ECO:0000313|EnsemblPlants:AES98352,
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 [3] {ECO:0000313|EMBL:AFK48498.1}
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 [4] {ECO:0000313|EMBL:AES98352.1, ECO:0000313|Proteomes:UP000002051}
RP GENOME REANNOTATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES98352,
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:AES98352}
RP IDENTIFICATION.
RC STRAIN=cv. Jemalong A17 {ECO:0000313|EnsemblPlants:AES98352};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
RN [6] {ECO:0000313|EMBL:RHN56320.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaves {ECO:0000313|EMBL:RHN56320.1};
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=(S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-
CC glutamyl-tRNA(Glu) + NADPH; Xref=Rhea:RHEA:12344, Rhea:RHEA-
CC COMP:9663, Rhea:RHEA-COMP:9680, ChEBI:CHEBI:15378, ChEBI:CHEBI:57501,
CC ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78520; EC=1.2.1.70;
CC Evidence={ECO:0000256|ARBA:ARBA00001415,
CC ECO:0000256|RuleBase:RU000584};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
CC {ECO:0000256|ARBA:ARBA00005059, ECO:0000256|RuleBase:RU000584}.
CC -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC {ECO:0000256|ARBA:ARBA00005916, ECO:0000256|RuleBase:RU000584}.
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DR EMBL; BT052932; ACJ85594.1; -; mRNA.
DR EMBL; CM001221; AES98352.1; -; Genomic_DNA.
DR EMBL; BT148704; AFK48498.1; -; mRNA.
DR EMBL; PSQE01000005; RHN56320.1; -; Genomic_DNA.
DR RefSeq; XP_003615394.1; XM_003615346.1.
DR AlphaFoldDB; B7FLG0; -.
DR STRING; 3880.B7FLG0; -.
DR PaxDb; 3880-AES98352; -.
DR EnsemblPlants; AES98352; AES98352; MTR_5g067410.
DR GeneID; 11421100; -.
DR Gramene; AES98352; AES98352; MTR_5g067410.
DR KEGG; mtr:11421100; -.
DR eggNOG; ENOG502QQ1H; Eukaryota.
DR HOGENOM; CLU_035113_2_1_1; -.
DR OMA; CDRIELW; -.
DR OrthoDB; 463at2759; -.
DR UniPathway; UPA00251; UER00316.
DR Proteomes; UP000002051; Chromosome 5.
DR Proteomes; UP000265566; Chromosome 5.
DR GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd05213; NAD_bind_Glutamyl_tRNA_reduct; 1.
DR Gene3D; 3.30.460.30; Glutamyl-tRNA reductase, N-terminal domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_00087; Glu_tRNA_reductase; 1.
DR InterPro; IPR000343; 4pyrrol_synth_GluRdtase.
DR InterPro; IPR015896; 4pyrrol_synth_GluRdtase_dimer.
DR InterPro; IPR015895; 4pyrrol_synth_GluRdtase_N.
DR InterPro; IPR018214; GluRdtase_CS.
DR InterPro; IPR036453; GluRdtase_dimer_dom_sf.
DR InterPro; IPR036343; GluRdtase_N_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase.
DR NCBIfam; TIGR01035; hemA; 1.
DR PANTHER; PTHR43120:SF16; GLUTAMYL-TRNA REDUCTASE; 1.
DR PANTHER; PTHR43120; GLUTAMYL-TRNA REDUCTASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00745; GlutR_dimer; 1.
DR Pfam; PF05201; GlutR_N; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR SUPFAM; SSF69742; Glutamyl tRNA-reductase catalytic, N-terminal domain; 1.
DR SUPFAM; SSF69075; Glutamyl tRNA-reductase dimerization domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00747; GLUTR; 1.
PE 2: Evidence at transcript level;
KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|RuleBase:RU000584};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000584};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244,
KW ECO:0000256|RuleBase:RU000584};
KW Reference proteome {ECO:0000313|Proteomes:UP000002051}.
FT DOMAIN 96..246
FT /note="Glutamyl-tRNA reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF05201"
FT DOMAIN 272..404
FT /note="Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA
FT reductase"
FT /evidence="ECO:0000259|Pfam:PF01488"
FT DOMAIN 418..522
FT /note="Tetrapyrrole biosynthesis glutamyl-tRNA reductase
FT dimerisation"
FT /evidence="ECO:0000259|Pfam:PF00745"
SQ SEQUENCE 542 AA; 59338 MW; C0F0F0C527868FCC CRC64;
MAVSTSFYGA KLEPLFLKCC SSSSTTSSSY VTTHLSFFGS NKKSFVQSRG SIRCDASSSD
VLIDPSDNAK SVSALQQLKA SAADRYTKER SSIVVIGLSI HTTPVDVREK LAIPEAEWPR
AIGELCNLNH IEEAAVLSTC NRMEIYVVAL SQHRGVKEVT EWMSNTSGIP ASELSKYLFL
LYNKDATQHL FEVSAGLDSL VMGEGQILSQ VKQVVKAGQG VNGFGRNISG LFKHAITVGK
RVRTETNIAA GAVSVSSAAV ELALMKLPDQ ASHGNARMLV IGAGKMGKLV IKHLVAKGCK
KMVVVNRTEG RVAAIREEIN DVEIIYKPLS EMLECIGEAD VVFTSTASEN PLIFKQNVKE
LPLASEEMGG KRLFVDISVP RNVGSCVDDL ESVKVYNVDD LKEVVAANKE DRLRKAMEAQ
VIIGEESGQF EAWRDSLETV PTIKKLRAYA ERLRVAELEK CLGKMGDDIN KKTQKAVDDL
SKGIVNKMLH GPMQHLRCDG SDSRTLSETL ENMHALNRMF SLETEVSVLE QKIRAKVEQK
PQ
//
