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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Paenarthrobacter aurescens (strain TC1)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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

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.UniRule annotation

Catalytic activityi

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

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase (hemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL)
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 sitei48NucleophileUniRule annotation1
Sitei100Important for activityUniRule annotation1
Binding sitei110SubstrateUniRule annotation1
Binding sitei121SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi192 – 197NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPorphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductaseUniRule annotation (EC:1.2.1.70UniRule annotation)
Short name:
GluTRUniRule annotation
Gene namesi
Name:hemAUniRule annotation
Ordered Locus Names:AAur_2756
OrganismiPaenarthrobacter aurescens (strain TC1)
Taxonomic identifieri290340 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaePaenarthrobacter
Proteomesi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003350091 – 440Glutamyl-tRNA reductaseAdd BLAST440

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi290340.AAur_2756

Structurei

3D structure databases

ProteinModelPortaliA1R8A6
SMRiA1R8A6
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni47 – 50Substrate bindingUniRule annotation4
Regioni115 – 117Substrate bindingUniRule annotation3

Domaini

Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.UniRule annotation

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105C7E Bacteria
COG0373 LUCA
HOGENOMiHOG000109649
KOiK02492
OrthoDBiPOG091H05DA

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
PIRSFiPIRSF000445 4pyrrol_synth_GluRdtase, 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.

A1R8A6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLFSLVATH ADIDLETVAQ LSNGSSELAS AALTDSSVVS GAVVLATCNR
60 70 80 90 100
YEVYGETANG ADLEAARSAL VSQISELSGL NEQLVSRSFA THTGPDVTRH
110 120 130 140 150
LFAVSAGLDS AVVGEREIAG QVRRALITAQ QEGTASSGLV RLFQAASKTA
160 170 180 190 200
KDVGAQTALG SRGLSIVSVA LDLATDLAEN DDWTTKKVVV FGTGAYAGAT
210 220 230 240 250
MSLLRERGCT DISVYSSSGR AEGFVATRGG TALDADTLPA AVAAADVMIG
260 270 280 290 300
CSGSDNRVEA ADLARVRANS GKPLIAIDLA LTHDFDPAVG ELDGVELLTL
310 320 330 340 350
ESVRLAAPQE QAESLSQASA IVNGAATSFE SEREARSVDT AIVALRRHTM
360 370 380 390 400
NVLDAEMEKV RARHGCTAAA EEVEFALRRM VKQLLHIPTV RARELAANGQ
410 420 430 440
QDDYVAALEA LYGIQVEQPQ AAAPASECPV DHEQLRSESA
Length:440
Mass (Da):45,893
Last modified:May 20, 2008 - v2
Checksum:iFC01F5CD3ADA7D8C
GO

Sequence cautioni

The sequence ABM08676 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000474 Genomic DNA Translation: ABM08676.1 Different initiation.
RefSeqiWP_014922283.1, NC_008711.1

Genome annotation databases

EnsemblBacteriaiABM08676; ABM08676; AAur_2756
GeneIDi29622867
KEGGiaau:AAur_2756

Entry informationi

Entry nameiHEM1_PAEAT
AccessioniPrimary (citable) accession number: A1R8A6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: March 28, 2018
This is version 86 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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