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Protein

Glutamyl-tRNA reductase 3, chloroplastic

Gene

HEMA3

Organism
Hordeum vulgare (Barley)
Status
Reviewed-Annotation score: -Experimental evidence at transcript leveli

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).By similarity

Miscellaneous

During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA (By similarity).By similarity

Catalytic activityi

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase 2 (HEMA2), Glutamyl-tRNA reductase 1, chloroplastic (HEMA1), Glutamyl-tRNA reductase 3, chloroplastic (HEMA3), Glutamyl-tRNA reductase (hemA1)
  2. Glutamate-1-semialdehyde 2,1-aminomutase, chloroplastic (GSA)
This subpathway is part of the pathway protoporphyrin-IX biosynthesis, which is itself part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu), the pathway protoporphyrin-IX biosynthesis and in Porphyrin-containing compound metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei131NucleophileBy similarity1
Sitei180Important for activityBy similarity1
Binding sitei190SubstrateBy similarity1
Binding sitei201SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi272 – 277NADPBy similarity6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processChlorophyll biosynthesis, Porphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase 3, chloroplastic (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:HEMA3
OrganismiHordeum vulgare (Barley)
Taxonomic identifieri4513 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBOP cladePooideaeTriticodaeTriticeaeHordeinaeHordeum

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_0000013312? – 535Glutamyl-tRNA reductase 3, chloroplastic
Transit peptidei1 – ?ChloroplastSequence analysis

Expressioni

Tissue specificityi

Primarily expressed in roots.

Gene expression databases

ExpressionAtlasiO65796 differential

Structurei

3D structure databases

ProteinModelPortaliO65796
SMRiO65796
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni131 – 133Substrate bindingBy similarity3
Regioni195 – 197Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IGX5 Eukaryota
COG0373 LUCA

Family and domain databases

Gene3Di3.30.460.30, 1 hit
HAMAPiMF_00087 Glu_tRNA_reductase, 1 hit
InterProiView protein in InterPro
IPR000343 4pyrrol_synth_GluRdtase
IPR015896 4pyrrol_synth_GluRdtase_dimer
IPR015895 4pyrrol_synth_GluRdtase_N
IPR018214 GluRdtase_CS
IPR036453 GluRdtase_dimer_dom_sf
IPR036343 GluRdtase_N_sf
IPR036291 NAD(P)-bd_dom_sf
IPR006151 Shikm_DH/Glu-tRNA_Rdtase
PfamiView protein in Pfam
PF00745 GlutR_dimer, 1 hit
PF05201 GlutR_N, 1 hit
PF01488 Shikimate_DH, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
SSF69075 SSF69075, 1 hit
SSF69742 SSF69742, 1 hit
TIGRFAMsiTIGR01035 hemA, 1 hit
PROSITEiView protein in PROSITE
PS00747 GLUTR, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O65796-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTSTASAT AMAGAFAAAG VNKPRGSAAC PRVPAGGRQR LSCVVRCDAG
60 70 80 90 100
PGVPAQMAAM AASVAALEQF KISADRYMKE KSSIAVIGLS IHTAPVEMRE
110 120 130 140 150
KLAVAEELWP RAVAELTNLN HIEKAAVLSP CNRMEIYVVA LSWNRGIREI
160 170 180 190 200
VDWMSMKSGI PAVELREHLF MFRDSDATRH LFEVSSGLDS LVLGEGQILA
210 220 230 240 250
QVKQVVRSGQ NSGGLGKNID RMFKDAITAG KRVRSETNIS CGAVSVSSAA
260 270 280 290 300
VELALMKLPK SECLSARMLL IGAGKMGRLV AKHLAAKGCK KVVIVNRSVE
310 320 330 340 350
RVDAIREEMQ GIEIVYRSLT EMYEAAADAD VVFTSTSSES PLFTKEHAEA
360 370 380 390 400
LPPVSGALGG VRLFVDISVP RNVSACVSDV GHARVYNVDD LKEVVEANKE
410 420 430 440 450
DRLRKAMEAQ TIISEELKRF EAWRDSMETV PTIKKLRSYA DRVRASELDK
460 470 480 490 500
CLQKIGEDAL TKKMRRSIEQ LSTGIVNRLL HGPLQHLRCD GTDNRTLDET
510 520 530
LENMHALNRM FGLDTEKAVM EQKIKTKVEK QKTQN
Length:535
Mass (Da):58,419
Last modified:August 1, 1998 - v1
Checksum:iB2830889AE6A3224
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D88383 mRNA Translation: BAA25168.1
PIRiT04402

Similar proteinsi

Entry informationi

Entry nameiHEM13_HORVU
AccessioniPrimary (citable) accession number: O65796
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: March 28, 2018
This is version 107 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health