ID   HEM12_HORVU             Reviewed;         465 AA.
AC   Q96563;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Glutamyl-tRNA reductase 2;
DE            Short=GluTR;
DE            EC=1.2.1.70;
DE   Flags: Fragment;
GN   Name=HEMA2;
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;
RX   PubMed=8696365; DOI=10.1046/j.1365-313x.1996.9060867.x;
RA   Bougri O., Grimm B.;
RT   "Members of a low-copy number gene family encoding glutamyl-tRNA reductase
RT   are differentially expressed in barley.";
RL   Plant J. 9:867-878(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.
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; X86102; CAA60055.1; -; mRNA.
DR   PIR; T05734; T05734.
DR   AlphaFoldDB; Q96563; -.
DR   SMR; Q96563; -.
DR   UniPathway; UPA00251; UER00316.
DR   ExpressionAtlas; Q96563; 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   PIRSF; PIRSF000445; 4pyrrol_synth_GluRdtase; 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.
FT   CHAIN           <1..465
FT                   /note="Glutamyl-tRNA reductase 2"
FT                   /id="PRO_0000114114"
FT   ACT_SITE        63
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         62..65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         127..129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         204..209
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250"
FT   SITE            112
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   465 AA;  51675 MW;  E42A50A3E749CE6D CRC64;
     QFKISADRYI KEKSSIAVIG LSVHTAPVDM REKLAVAEEL WPRAISELTS LNHIEEAAVL
     STCNRMEIYV VALSWNRGIR EVVDWMSKKS GIPASELREH LFMLRDSGAT RHLFEVSAGL
     DSLVLGEGQI LAQVKQVVRN GQNSGGLGKN IDRMFKDAIT AGKRARCETN ISAGAVSVSS
     AAVELAMMKL PKSECLSARM LLIGAGKMGK LVVKHLIAKG CKKVVVVNRS VERVDAIREE
     MKDIEIVYRP LTEMYEAAAD ADVVFTSTAS ESLLFTKEHA EALPPISLAM GGVRLFVDIS
     VPRNVGACLS QVEHARVYNV DDLKEVVEAN KEDRVRKAME AQAIITQELK RFEAWRDSLE
     TVPTIKKLRS YADRIRASEL DKCLQKIGED NLNKKTRRSI EELSTGIVNK LLHGPLQHLR
     CDGSDSRTLD ETLDNMHALN RMFNLDTEKA VLEQKIKAKV EKTQS