HEM11_HORVU
ID HEM11_HORVU Reviewed; 527 AA.
AC Q42843; Q42844;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Glutamyl-tRNA reductase 1, chloroplastic;
DE Short=GluTR;
DE EC=1.2.1.70;
DE Flags: Precursor;
GN Name=HEMA1;
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. Klages;
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).
RN [2]
RP PROTEIN SEQUENCE OF 44-65, AND CHARACTERIZATION.
RX PubMed=7957167; DOI=10.1111/j.1432-1033.1994.00529.x;
RA Pontoppidan B., Kannangara C.G.;
RT "Purification and partial characterisation of barley glutamyl-tRNA(Glu)
RT reductase, the enzyme that directs glutamate to chlorophyll biosynthesis.";
RL Eur. J. Biochem. 225:529-537(1994).
RN [3]
RP FUNCTION, CHARACTERIZATION, HEME BINDING, AND SUBUNIT.
RX PubMed=8799193; DOI=10.1073/pnas.93.17.9287;
RA Vothknecht U.C., Kannangara C.G., von Wettstein D.;
RT "Expression of catalytically active barley glutamyl tRNAGlu reductase in
RT Escherichia coli as a fusion protein with glutathione S-transferase.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:9287-9291(1996).
RN [4]
RP 3D-STRUCTURE MODELING OF 76-460.
RX PubMed=10591107;
RX DOI=10.1002/(sici)1097-0134(19991115)37:3<485::aid-prot15>3.0.co;2-g;
RA Brody S.S., Gough S.P., Kannangara C.G.;
RT "Predicted structure and fold recognition for the glutamyl tRNA reductase
RT family of proteins.";
RL Proteins 37:485-493(1999).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu)
CC to glutamate 1-semialdehyde (GSA). {ECO:0000269|PubMed:8799193}.
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 -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8799193}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- MISCELLANEOUS: Was shown to bind heme, but the precise role of heme is
CC unclear.
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=CAA60054.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X92403; CAA63140.1; -; mRNA.
DR EMBL; X86101; CAA60054.1; ALT_INIT; mRNA.
DR PIR; T05732; T05732.
DR AlphaFoldDB; Q42843; -.
DR SMR; Q42843; -.
DR EnsemblPlants; HORVU.MOREX.r2.1HG0037430.1; HORVU.MOREX.r2.1HG0037430.1; HORVU.MOREX.r2.1HG0037430.
DR EnsemblPlants; HORVU.MOREX.r2.1HG0037430.1.mrna1; HORVU.MOREX.r2.1HG0037430.1.mrna1; HORVU.MOREX.r2.1HG0037430.1.
DR Gramene; HORVU.MOREX.r2.1HG0037430.1; HORVU.MOREX.r2.1HG0037430.1; HORVU.MOREX.r2.1HG0037430.
DR Gramene; HORVU.MOREX.r2.1HG0037430.1.mrna1; HORVU.MOREX.r2.1HG0037430.1.mrna1; HORVU.MOREX.r2.1HG0037430.1.
DR KEGG; ag:CAA63140; -.
DR BRENDA; 1.2.1.70; 2687.
DR UniPathway; UPA00251; UER00316.
DR ExpressionAtlas; Q42843; 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 1: Evidence at protein level;
KW Chlorophyll biosynthesis; Chloroplast; Direct protein sequencing; NADP;
KW Oxidoreductase; Plastid; Porphyrin biosynthesis; Transit peptide.
FT TRANSIT 1..43
FT /note="Chloroplast"
FT /evidence="ECO:0000269|PubMed:7957167"
FT CHAIN 44..527
FT /note="Glutamyl-tRNA reductase 1, chloroplastic"
FT /id="PRO_0000013311"
FT ACT_SITE 125
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 124..127
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 189..191
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 195
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 266..271
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250"
FT SITE 174
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 527 AA; 57653 MW; D329E56458BE1165 CRC64;
MAGATSATAA AGAFAAAKAR GPAAACPWLV AAGGRRRSGV VRCDAGGDAQ AASKAASITA
LEQFKISADR YMKEKSSIAV IGLSVHTAPV EMREKLAVAE ELWPRAISEL TSLNHIEEAA
VLSTCNRMEI YVVALSWNRG IREVVDWMSK KSGIPASELR EHLFMLRDSD ATRHLFEVSA
GLDSLVLGEG QILAQVKQVV RNGQNSGGLG KNIDRMFKDA ITAGKRVRCE TNISAGAVSV
SSAAVELAMM KLPKSECLSA RMLLIGAGKM GKLVVKHLIA KGCKKVVVVN RSVERVDAIR
EEMKDIEIVY RPLTEMYEAA ADADVVFTST ASESLLFTKE HAEVLPPISL AMGGVRLFVD
ISVPRNVGAC LSEVEHARVY NVDDLKEVVE ANKEDRVRKA MEAQTIITQE LKRFEAWRDS
LETVPTIKKL RSYADRIRAS ELEKCLQKIG EDNLNKKMRR SIEELSTGIV NKLLHGPLQH
LRCDGSDSRT LDETLENMHA LNRMFSLDTE KAVLEQKIKA KVEKTQS
