ID   HEM1_ORYSI              Reviewed;         537 AA.
AC   A2Z928; O48674; Q0IWL0; Q337F6; Q8LNE9; Q9FW00;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   13-SEP-2023, entry version 92.
DE   RecName: Full=Glutamyl-tRNA reductase, chloroplastic;
DE            Short=GluTR;
DE            EC=1.2.1.70;
DE   Flags: Precursor;
GN   ORFNames=OsI_033071;
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. IR36;
RA   Nakayashiki T., Inokuchi H.;
RT   "Nucleotide sequence of a cDNA clone encoding glutamyl-tRNA reductase from
RT   rice.";
RL   (er) Plant Gene Register PGR98-080(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
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   -!- 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA25003.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=EAY79112.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB011416; BAA25003.1; ALT_FRAME; mRNA.
DR   EMBL; CM000135; EAY79112.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A2Z928; -.
DR   SMR; A2Z928; -.
DR   STRING; 39946.A2Z928; -.
DR   HOGENOM; CLU_035113_2_1_1; -.
DR   UniPathway; UPA00251; UER00316.
DR   Proteomes; UP000007015; Chromosome 10.
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   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; GLUTAMYL-TRNA REDUCTASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43120:SF1; 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; Reference proteome; Transit peptide.
FT   TRANSIT         1..48
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           49..537
FT                   /note="Glutamyl-tRNA reductase, chloroplastic"
FT                   /id="PRO_0000295656"
FT   ACT_SITE        135
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         134..137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         199..201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         276..281
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            184
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        151
FT                   /note="I -> L (in Ref. 1; BAA25003)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        201
FT                   /note="Q -> E (in Ref. 1; BAA25003)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        463
FT                   /note="S -> A (in Ref. 1; BAA25003)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        468
FT                   /note="M -> T (in Ref. 1; BAA25003)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   537 AA;  58435 MW;  51414A99FFF50A9A CRC64;
     MMASTTSATA AGGAFAAAKT RAGSSAAGGG ACARVAAGGR RRSGVVVRCD AGVEAQAQAQ
     AVAKAASVAA LEQFKISADR YMKERSSIAV IGLSVHTAPV EMREKLAVAE ELWPRAISEL
     TSLNHIEEAA VLSTCNRMEI YVVALSWNRG IREVVDWMSK KSGIPASELR EHLFMLRDSD
     ATRHLFEVSA GLDSLVLGEG QILAQVKQVV RSGQNSGGLG KNIDRMFKDA ITAGKRVRCE
     TNISSGAVSV SSAAVELALM KLPKSECLSA RMLLIGAGKM GKLVVKHLIA KGCKKVVVVN
     RSVERVDAIR EEMKDIEIVY RPLTEMYEAA AEADVVFTST ASETPLFTKE HAEALPAISD
     AMGGVRLFVD ISVPRNVSAC VSEVGHARVY NVDDLKEVVE ANKEDRLRKA MEAQTIITQE
     LKRFEAWRDS LETVPTIKKL RSYADRIRAS ELEKCLQKIG EDSLTKKMRR SIEELSTGIV
     NKLLHGPLQH LRCDGSDSRT LDETLENMHA LNRMFSLDTE KAIIEQKIKA KVEKSQN
//