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Protein

Glutamyl-tRNA reductase 1, chloroplastic

Gene

HEMA1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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_At1g52270), Glutamyl-tRNA reductase (AXX17_At2g27450), 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
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Chlorophyll biosynthesis, Porphyrin biosynthesis

Keywords - Ligandi

NADP

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

TAIRiAT1G58290.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast membrane Source: UniProtKB-SubCell
  • protein complex Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 64ChloroplastSequence analysisAdd BLAST64
ChainiPRO_000001330765 – 543Glutamyl-tRNA reductase 1, chloroplasticAdd BLAST479

Proteomic databases

PaxDbiP42804.

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

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.
MINTiMINT-8300920.
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.
OMAiCELKAME.
OrthoDBiEOG093609MY.
PhylomeDBiP42804.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase. 1 hit.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

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.

Cross-referencesi

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.

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...

Protein-protein interaction databases

BioGridi27423. 5 interactors.
IntActiP42804. 4 interactors.
MINTiMINT-8300920.
STRINGi3702.AT1G58290.1.

Proteomic databases

PaxDbiP42804.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT1G58290.

Phylogenomic databases

eggNOGiENOG410IGX5. Eukaryota.
COG0373. LUCA.
HOGENOMiHOG000109651.
InParanoidiP42804.
KOiK02492.
OMAiCELKAME.
OrthoDBiEOG093609MY.
PhylomeDBiP42804.

Enzyme and pathway databases

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

Miscellaneous databases

PROiP42804.

Gene expression databases

GenevisibleiP42804. AT.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase. 1 hit.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHEM11_ARATH
AccessioniPrimary (citable) accession number: P42804
Secondary accession number(s): Q0WWL6, Q9LQB9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: April 3, 2002
Last modified: November 30, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.