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   25-NOV-2008, entry version 60.
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; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids I; Cucurbitales; Cucurbitaceae; Cucumis.
OX   NCBI_TaxID=3659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Aonagajibai; TISSUE=Cotyledon;
RX   MEDLINE=97088717; PubMed=8934625; DOI=10.1104/pp.110.4.1223;
RA   Tanaka R., Yoshida K., Nakayashiki T., Masuda T., Tsuji H.,
RA   Inokuchi H., Tanaka A.;
RT   "Differential expression of two hemA mRNAs encoding glutamyl-tRNA
RT   reductase proteins in greening cucumber seedlings.";
RL   Plant Physiol. 110:1223-1230(1996).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-
CC       tRNA(Glu) to glutamate 1-semialdehyde (GSA) (By similarity).
CC   -!- CATALYTIC ACTIVITY: L-glutamate 1-semialdehyde + NADP(+) +
CC       tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.
CC   -!- PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-
CC       aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast (By similarity).
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
CC       glutamate with the formation of a thioester intermediate between
CC       enzyme and glutamate, and the concomitant release of tRNA(Glu).
CC       The thioester intermediate is finally reduced by direct hydride
CC       transfer from NADPH, to form the product GSA (By similarity).
CC   -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family.
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DR   EMBL; D67088; BAA11091.1; -; mRNA.
DR   PIR; T10245; T10245.
DR   HSSP; Q9UXR8; 1GPJ.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-KW.
DR   GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0004764; F:shikimate 5-dehydrogenase activity; IEA:InterPro.
DR   GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR000343; 4pyrrol_synth_GluRdtase.
DR   InterPro; IPR015896; 4pyrrol_synth_GluRdtase_C.
DR   InterPro; IPR015895; 4pyrrol_synth_GluRdtase_N.
DR   InterPro; IPR016040; NAD(P)-bd.
DR   InterPro; IPR006151; Shikm_DHase/Glu-tRNA_Rdtase.
DR   Gene3D; G3DSA:3.40.50.720; NAD(P)-bd; 1.
DR   Pfam; PF00745; GlutR_dimer; 1.
DR   Pfam; PF05201; GlutR_N; 1.
DR   Pfam; PF01488; Shikimate_DH; 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      ?       Chloroplast (Potential).
FT   CHAIN         ?    542       Glutamyl-tRNA reductase 2, chloroplastic.
FT                                /FTId=PRO_0000013310.
FT   NP_BIND     284    289       NADP (By similarity).
FT   REGION      142    145       Substrate binding (By similarity).
FT   REGION      207    209       Substrate binding (By similarity).
FT   ACT_SITE    143    143       Nucleophile (By similarity).
FT   BINDING     202    202       Substrate (By similarity).
FT   BINDING     213    213       Substrate (By similarity).
FT   SITE        192    192       Important for activity (By similarity).
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
//