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Protein

Glutamyl-tRNA reductase 1, chloroplastic

Gene

HEMA1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). Probably involved in the tetrapyrrole synthesis required for the chlorophyll biosynthesis.2 Publications

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.1 Publication

Enzyme regulationi

Negatively regulated by FLU and heme.2 Publications

Pathwayi: chlorophyll biosynthesis

This protein is involved in the pathway chlorophyll biosynthesis, which is part of Porphyrin-containing compound metabolism.
View all proteins of this organism that are known to be involved in the pathway chlorophyll biosynthesis and in Porphyrin-containing compound metabolism.

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 (AXX17_At1g09980), Glutamyl-tRNA reductase 2, chloroplastic (HEMA2), Glutamyl-tRNA reductase 1, chloroplastic (HEMA1), Glutamyl-tRNA reductase (AXX17_At2g27450), Glutamyl-tRNA reductase (AXX17_At1g52270), Probable glutamyl-tRNA reductase 3, chloroplastic (HEMA3)
  2. Glutamate-1-semialdehyde 2,1-aminomutase 1, chloroplastic (GSA1), Glutamate-1-semialdehyde 2,1-aminomutase 2, chloroplastic (GSA2)
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 sitei144NucleophileBy similarity1
Sitei193Important for activityBy similarity1
Binding sitei203SubstrateBy similarity1
Binding sitei214SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi285 – 290NADPBy similarity6

GO - Molecular functioni

  • glutamyl-tRNA reductase activity Source: TAIR
  • NADP binding Source: InterPro

GO - Biological processi

  • chlorophyll biosynthetic process Source: TAIR
  • heme biosynthetic process Source: TAIR
  • protoporphyrinogen IX biosynthetic process Source: UniProtKB-UniPathway

Keywordsi

Molecular functionOxidoreductase
Biological processChlorophyll biosynthesis, Porphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

BioCyciARA:AT1G58290-MONOMER
MetaCyc:AT1G58290-MONOMER
UniPathwayiUPA00251; UER00316
UPA00668

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase 1, chloroplastic (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:HEMA1
Synonyms:HEMA
Ordered Locus Names:At1g58290
ORF Names:F19C14.9
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

AraportiAT1G58290
TAIRilocus:2016605 AT1G58290

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, Membrane, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 61ChloroplastCuratedAdd BLAST61
ChainiPRO_000001330762 – 543Glutamyl-tRNA reductase 1, chloroplasticAdd BLAST482

Proteomic databases

PaxDbiP42804
PRIDEiP42804

Expressioni

Tissue specificityi

Strongly expressed in photosynthetic tissues. Detected in all tissues tested.3 Publications

Inductioni

Circadian-regulation. Up-regulated by light.4 Publications

Gene expression databases

ExpressionAtlasiP42804 baseline and differential
GenevisibleiP42804 AT

Interactioni

Subunit structurei

Part of the FLU-containing chloroplast membrane complex composed of FLU, CRD1, PORB, PORC, CHLP and HEMA1. Interacts (via C-terminus) with FLU, only in the absence of light. Interacts with GLUTRBP and forms a heterotetramer of two GLUTRBP and two HEMA1 subunits. Interacts with CLPF (PubMed:26419670).5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FLUQ940U63EBI-2319900,EBI-2319882

Protein-protein interaction databases

BioGridi27423, 5 interactors
IntActiP42804, 4 interactors
MINTiP42804
STRINGi3702.AT1G58290.1

Structurei

Secondary structure

1543
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi96 – 103Combined sources8
Turni104 – 106Combined sources3
Helixi109 – 115Combined sources7
Helixi119 – 121Combined sources3
Helixi122 – 131Combined sources10
Beta strandi135 – 143Combined sources9
Beta strandi146 – 155Combined sources10
Helixi156 – 171Combined sources16
Helixi175 – 181Combined sources7
Beta strandi183 – 186Combined sources4
Helixi188 – 198Combined sources11
Beta strandi202 – 205Combined sources4
Beta strandi207 – 209Combined sources3
Helixi211 – 222Combined sources12
Beta strandi226 – 228Combined sources3
Helixi230 – 248Combined sources19
Turni252 – 255Combined sources4
Helixi259 – 270Combined sources12
Beta strandi273 – 276Combined sources4
Beta strandi281 – 284Combined sources4
Helixi288 – 299Combined sources12
Beta strandi304 – 310Combined sources7
Helixi312 – 321Combined sources10
Beta strandi325 – 331Combined sources7
Helixi332 – 334Combined sources3
Helixi335 – 340Combined sources6
Beta strandi343 – 347Combined sources5
Helixi358 – 362Combined sources5
Helixi369 – 371Combined sources3
Beta strandi375 – 379Combined sources5
Helixi388 – 392Combined sources5
Beta strandi396 – 400Combined sources5
Helixi401 – 407Combined sources7
Turni414 – 416Combined sources3
Helixi417 – 439Combined sources23
Helixi440 – 442Combined sources3
Helixi443 – 466Combined sources24
Turni467 – 470Combined sources4
Helixi474 – 497Combined sources24
Helixi509 – 523Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4N7RX-ray2.80A/B73-543[»]
4YVQX-ray2.40A440-543[»]
5CHEX-ray3.20A/B73-543[»]
ProteinModelPortaliP42804
SMRiP42804
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni143 – 146Substrate bindingBy similarity4
Regioni208 – 210Substrate bindingBy similarity3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi23 – 33Poly-SerAdd BLAST11
Compositional biasi305 – 308Poly-Val4

Domaini

The N-terminus (65-92) is required for heme inhibition, but not for activity.1 Publication

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiENOG410IGX5 Eukaryota
COG0373 LUCA
HOGENOMiHOG000109651
InParanoidiP42804
KOiK02492
OMAiFAFKCAA
OrthoDBiEOG093609MY
PhylomeDBiP42804

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.

P42804-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVSSAFVGC PKLETLLNHH NLSPSSSSSS SVSQTPLGLN GVRVLPKNNR
60 70 80 90 100
TRRGLIQKAR CELSASSDSA SNAASISALE QLKNSAADRY TKERSSIVVI
110 120 130 140 150
GLSIHTAPVE MREKLAIPEA EWPRAIAELC GLNHIEEAAV LSTCNRMEIY
160 170 180 190 200
VLALSQHRGV KEVTEWMSKT SGIPVSEICQ HRFLLYNKDA TQHIFEVSAG
210 220 230 240 250
LDSLVLGEGQ ILAQVKQVVK VGQGVNGFGR NISGLFKHAI TVGKRVRTET
260 270 280 290 300
NIASGAVSVS SAAVELALMK LPQSSNVSAR MCVIGAGKMG KLVIKHLMAK
310 320 330 340 350
GCTKVVVVNR SEERVSAIRE EMPGIEIIYR PLDEMLACAS EADVVFTSTA
360 370 380 390 400
SETPLFLKEH VENLPQASPE VGGLRHFVDI SVPRNVGSCV GEVETARVYN
410 420 430 440 450
VDDLKEVVAA NKEDRMRKAM EAQTIITEES TQFEAWRDSL ETVPTIKKLR
460 470 480 490 500
AYAERIRVAE LEKCMSKMGD DINKKTTRAV DDLSRGIVNR FLHGPMQHLR
510 520 530 540
CDGSDSRTLS ETLENMHALN RMYGLEKDIL EEKLKAMAEQ QQK
Length:543
Mass (Da):59,515
Last modified:April 3, 2002 - v2
Checksum:i04A095FEC96CC014
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti62E → V in AAA19118 (PubMed:7908550).Curated1
Sequence conflicti169K → N in AAA19118 (PubMed:7908550).Curated1
Sequence conflicti291K → L in AAA19118 (PubMed:7908550).Curated1
Sequence conflicti443V → G in BAE98482 (Ref. 5) Curated1
Sequence conflicti542Q → H in AAA19118 (PubMed:7908550).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U03774 Genomic DNA Translation: AAA19118.1
AC008051 Genomic DNA Translation: AAF82258.1
CP002684 Genomic DNA Translation: AEE33532.1
AY072223 mRNA Translation: AAL60044.1
AY096600 mRNA Translation: AAM20250.1
AK226332 mRNA Translation: BAE98482.1
PIRiE96616
RefSeqiNP_176125.1, NM_104609.4
UniGeneiAt.241

Genome annotation databases

EnsemblPlantsiAT1G58290.1; AT1G58290.1; AT1G58290
GeneIDi842198
GrameneiAT1G58290.1; AT1G58290.1; AT1G58290
KEGGiath:AT1G58290

Similar proteinsi

Entry informationi

Entry nameiHEM11_ARATH
AccessioniPrimary (citable) accession number: P42804
Secondary accession number(s): Q0WWL6, Q9LQB9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 3, 2002
Last modified: May 23, 2018
This is version 156 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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