ID   HEM12_CUCSA             Reviewed;         542 AA.
AC   P49295;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   02-SEP-2026, entry version 120.
DE   RecName: Full=Glutamyl-tRNA reductase 2, chloroplastic;
DE            Short=GluTR;
DE            EC=1.2.1.70;
DE   Flags: Precursor;
GN   Name=HEMA2;
OS   Cucumis sativus (Cucumber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Aonagajibai; TISSUE=Cotyledon;
RX   PubMed=8934625; DOI=10.1104/pp.110.4.1223;
RA   Tanaka R., Yoshida K., Nakayashiki T., Masuda T., Tsuji H., Inokuchi H.,
RA   Tanaka A.;
RT   "Differential expression of two hemA mRNAs encoding glutamyl-tRNA reductase
RT   proteins in greening cucumber seedlings.";
RL   Plant Physiol. 110:1223-1230(1996).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu)
CC       to glutamate 1-semialdehyde (GSA). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-4-amino-5-oxopentanoate + tRNA(Glu) + NADP(+) = L-
CC         glutamyl-tRNA(Glu) + NADPH + H(+); 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   -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC       biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Found in all tissues examined.
CC   -!- MISCELLANEOUS: During catalysis, the active site Cys acts as a
CC       nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate
CC       with the formation of a thioester intermediate between enzyme and
CC       glutamate, and the concomitant release of tRNA(Glu). The thioester
CC       intermediate is finally reduced by direct hydride transfer from NADPH,
CC       to form the product GSA (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
CC       {ECO:0000305}.
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DR   EMBL; D67088; BAA11091.1; -; mRNA.
DR   PIR; T10245; T10245.
DR   RefSeq; NP_001267616.1; NM_001280687.1.
DR   AlphaFoldDB; P49295; -.
DR   SMR; P49295; -.
DR   GeneID; 101208135; -.
DR   KEGG; csv:101208135; -.
DR   eggNOG; ENOG502QQ1H; Eukaryota.
DR   OrthoDB; 424281at2759; -.
DR   UniPathway; UPA00251; UER00316.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-ARBA.
DR   CDD; cd05213; NAD_bind_Glutamyl_tRNA_reduct; 1.
DR   FunFam; 3.30.460.30:FF:000001; Glutamyl-tRNA reductase; 1.
DR   FunFam; 3.40.50.720:FF:000031; Glutamyl-tRNA reductase; 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:SF4; 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   Chlorophyll biosynthesis; Chloroplast; NADP; Oxidoreductase; Plastid;
KW   Porphyrin biosynthesis; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..542
FT                   /note="Glutamyl-tRNA reductase 2, chloroplastic"
FT                   /id="PRO_0000013310"
FT   ACT_SITE        143
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         142..145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         207..209
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         284..289
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            192
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   542 AA;  59707 MW;  A576B3B96A0B6EEF CRC64;
     MAAAVGGLTT CFARPTPEFI APSTSYSAPV RVFFKPFKVR DLCCAGEVVG VLSARSIPIS
     PRFELIRLVR MQPGLSALEL LKTSSVNRYT KERISIVVIG LNVHTAPVEL REKLAIPEAQ
     WPPGIGELCA LNHIEEAAVL STCNRIEIYV VALSQHRGVK EVTEWMSKRS GIPISELCKH
     RVLLYNTDAT QHLFEVSAGL DSLVLGEGQI LAQVKHVVKT GQGVAGFDRK ISGLFKHAIT
     VGKRVRTETN ISSGSFSVSS AAVELAQKKL PESSYATAKV MVVGAGKMGK LVIKHLVAKG
     CRKMVVVNRT QDSVDAVEEL KDVEIIYKPL SKILACASEA DVIFTCTASK TPLFTKEHVA
     MLPPAGTETG RRLFVDISVP RNVEQRVSDL ETVSVFNVDD LKEVVAANKE DRLKKVQEAQ
     SIIGEEINKF EAWRDSLETV PTIKKFRAYV ERIRAAELDK CLSKMGEDIP KKKKVAINDL
     SLGIANKLLH GPIQHLRCDG NDSRTLDEIL QNMHAINRMF DLETDLSVLE EKIRAKVERG
     QK
//