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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Thiobacillus denitrificans (strain ATCC 25259)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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 sitei50NucleophileUniRule annotation1
Sitei95Important for activityUniRule annotation1
Binding sitei105SubstrateUniRule annotation1
Binding sitei116SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi185 – 190NADPUniRule 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:Tbd_2492
OrganismiThiobacillus denitrificans (strain ATCC 25259)
Taxonomic identifieri292415 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesThiobacillaceaeThiobacillus
Proteomesi
  • UP000008291 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003350781 – 416Glutamyl-tRNA reductaseAdd BLAST416

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi292415.Tbd_2492.

Structurei

3D structure databases

ProteinModelPortaliQ3SG11.
SMRiQ3SG11.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni49 – 52Substrate bindingUniRule annotation4
Regioni110 – 112Substrate 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.
OrthoDBiPOG091H05DA.

Family and domain databases

Gene3Di1.10.1200.70. 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.

Q3SG11-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQLLTLGVNH HTAPLAIREQ VAFGPDKLVQ ALHELTLSKR ASEAAILSTC
60 70 80 90 100
NRTELYVNTV SPDALSQWFA DFHHLDVREL APYLYTLPRE KAAQHAFRVA
110 120 130 140 150
AGLDSMVLGE TQILGQMKQA VAAAEEAGTL GLLLHKLFQR TFSVAKEVRS
160 170 180 190 200
STEIGANSVS MAAAAVRLAE RIFPSVKEQA CLFIGAGEMI ELCMTHFAAQ
210 220 230 240 250
HPRRMTVANR TTERARPLAE RFNAGVIPLT ALPDEVAAYD IIITSTASPL
260 270 280 290 300
PILGKGMLER AIRQRRHRPI FIVDLAVPRD VEAEVADMND VFLYSVDDLG
310 320 330 340 350
QVVREGMDNR VAQVAQAEAI IETSVASFIH WMEGRELVPV IRGLRDAAER
360 370 380 390 400
HRRHELDKAH KALARGDDPH AVLDAMSHGL ANKFLHAPTH GLSHATPEER
410
AELVRLISQL YGLHPE
Length:416
Mass (Da):45,872
Last modified:October 11, 2005 - v1
Checksum:i6ADDDBD3E9427BCA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000116 Genomic DNA. Translation: AAZ98445.1.
RefSeqiWP_011313004.1. NC_007404.1.

Genome annotation databases

EnsemblBacteriaiAAZ98445; AAZ98445; Tbd_2492.
KEGGitbd:Tbd_2492.

Similar proteinsi

Entry informationi

Entry nameiHEM1_THIDA
AccessioniPrimary (citable) accession number: Q3SG11
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 11, 2005
Last modified: October 25, 2017
This is version 93 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