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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
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 sitei47NucleophileUniRule annotation1
Sitei86Important for activityUniRule annotation1
Binding sitei96SubstrateUniRule annotation1
Binding sitei107SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi176 – 181NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPorphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

BioCyciTTHE300852:G1GKC-1512-MONOMER
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:TTHA1506
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000047171 – 390Glutamyl-tRNA reductaseAdd BLAST390

Proteomic databases

PRIDEiQ5SI68

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi300852.TTHA1506

Structurei

3D structure databases

ProteinModelPortaliQ5SI68
SMRiQ5SI68
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni46 – 49Substrate bindingUniRule annotation4
Regioni101 – 103Substrate 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
HOGENOMiHOG000109650
KOiK02492
OMAiFAFKCAA
PhylomeDBiQ5SI68

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
IPR015895 4pyrrol_synth_GluRdtase_N
IPR018214 GluRdtase_CS
IPR036343 GluRdtase_N_sf
IPR036291 NAD(P)-bd_dom_sf
IPR006151 Shikm_DH/Glu-tRNA_Rdtase
PfamiView protein in Pfam
PF05201 GlutR_N, 1 hit
PF01488 Shikimate_DH, 1 hit
PIRSFiPIRSF000445 4pyrrol_synth_GluRdtase, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
SSF69742 SSF69742, 1 hit
TIGRFAMsiTIGR01035 hemA, 1 hit
PROSITEiView protein in PROSITE
PS00747 GLUTR, 1 hit

Sequencei

Sequence statusi: Complete.

Q5SI68-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALPLYLVGL SHKTAPLEVR ERAALDPVVA LPAALSALGK GVVLSTCNRT
60 70 80 90 100
ELYGVGSPEK ARAFLLSRGV APRHLYVKEG VEALRHLYRV AAGLDSLVVG
110 120 130 140 150
EAQILGQVRE ALFLARRQGA TESLLEKAFQ SAIALGKRAR SETGIGMGAV
160 170 180 190 200
SVAYAALDLA LAVYGDLSGL SVAVLGAGEM AELFLTHLKA HGVGRILVVN
210 220 230 240 250
RTEEKAQALA ERFGGEAFGL PALPQVLRQA DLVVASAAAP HYLVGPEDLP
260 270 280 290 300
KRAKPLFLID IALPRNIDPR VGDLPHAYLY NLDDLKRVVD RNLRARAGEI
310 320 330 340 350
PKVEALIEKA LGDYMEWYAG HRVREAIRAL EAWARVQAAK AQPEAGPVEL
360 370 380 390
EKAAGRLAHP FILGLKRRAL DRVGGPPCPE DCLLYRLSRT
Length:390
Mass (Da):41,937
Last modified:December 21, 2004 - v1
Checksum:iA0B5EF3A10C5DD15
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA Translation: BAD71329.1
RefSeqiWP_011228725.1, NC_006461.1
YP_144772.1, NC_006461.1

Genome annotation databases

EnsemblBacteriaiBAD71329; BAD71329; BAD71329
GeneIDi3168904
KEGGittj:TTHA1506
PATRICifig|300852.9.peg.1481

Similar proteinsi

Entry informationi

Entry nameiHEM1_THET8
AccessioniPrimary (citable) accession number: Q5SI68
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: December 21, 2004
Last modified: May 23, 2018
This is version 96 of the entry and version 1 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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