HEM12_CUCSA
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 03-AUG-2022, entry version 113.
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 + 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 -!- 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 STRING; 3659.XP_004155425.1; -.
DR GeneID; 101208135; -.
DR KEGG; csv:101208135; -.
DR eggNOG; ENOG502QQ1H; Eukaryota.
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:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.460.30; -; 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 Pfam; PF00745; GlutR_dimer; 1.
DR Pfam; PF05201; GlutR_N; 1.
DR Pfam; PF01488; Shikimate_DH; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF69075; SSF69075; 1.
DR SUPFAM; SSF69742; SSF69742; 1.
DR TIGRFAMs; TIGR01035; hemA; 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
