ID   HEM13_HORVU             Reviewed;         535 AA.
AC   O65796;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Glutamyl-tRNA reductase 3, chloroplastic;
DE            Short=GluTR;
DE            EC=1.2.1.70;
DE   Flags: Precursor;
GN   Name=HEMA3;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Bonus; TISSUE=Root;
RA   Tanaka R., Yoshida K., Nakayashiki T., Tsuji H., Inokuchi H., Okada K.,
RA   Tanaka A.;
RT   "The third member of the hemA gene family encoding glutamyl-tRNA reductase
RT   is primarily expressed in roots in Hordeum vulgare.";
RL   Photosyn. Res. 53:161-171(1997).
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.
CC   -!- TISSUE SPECIFICITY: Primarily expressed in roots.
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; D88383; BAA25168.1; -; mRNA.
DR   PIR; T04402; T04402.
DR   AlphaFoldDB; O65796; -.
DR   SMR; O65796; -.
DR   UniPathway; UPA00251; UER00316.
DR   ExpressionAtlas; O65796; baseline and differential.
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           ?..535
FT                   /note="Glutamyl-tRNA reductase 3, chloroplastic"
FT                   /id="PRO_0000013312"
FT   ACT_SITE        131
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         131..133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         195..197
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         272..277
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            180
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   535 AA;  58419 MW;  B2830889AE6A3224 CRC64;
     MASTSTASAT AMAGAFAAAG VNKPRGSAAC PRVPAGGRQR LSCVVRCDAG PGVPAQMAAM
     AASVAALEQF KISADRYMKE KSSIAVIGLS IHTAPVEMRE KLAVAEELWP RAVAELTNLN
     HIEKAAVLSP CNRMEIYVVA LSWNRGIREI VDWMSMKSGI PAVELREHLF MFRDSDATRH
     LFEVSSGLDS LVLGEGQILA QVKQVVRSGQ NSGGLGKNID RMFKDAITAG KRVRSETNIS
     CGAVSVSSAA VELALMKLPK SECLSARMLL IGAGKMGRLV AKHLAAKGCK KVVIVNRSVE
     RVDAIREEMQ GIEIVYRSLT EMYEAAADAD VVFTSTSSES PLFTKEHAEA LPPVSGALGG
     VRLFVDISVP RNVSACVSDV GHARVYNVDD LKEVVEANKE DRLRKAMEAQ TIISEELKRF
     EAWRDSMETV PTIKKLRSYA DRVRASELDK CLQKIGEDAL TKKMRRSIEQ LSTGIVNRLL
     HGPLQHLRCD GTDNRTLDET LENMHALNRM FGLDTEKAVM EQKIKTKVEK QKTQN