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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Pseudomonas fluorescens (strain SBW25)
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
Sitei97Important for activityUniRule annotation1
Binding sitei107SubstrateUniRule annotation1
Binding sitei118SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi187 – 192NADPUniRule 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:PFLU_0737
OrganismiPseudomonas fluorescens (strain SBW25)
Taxonomic identifieri216595 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002332 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10002026401 – 429Glutamyl-tRNA reductaseAdd BLAST429

Proteomic databases

PRIDEiC3KDC5.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi216595.PFLU0737.

Structurei

3D structure databases

ProteinModelPortaliC3KDC5.
SMRiC3KDC5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni49 – 52Substrate bindingUniRule annotation4
Regioni112 – 114Substrate 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.
KOiK02492.
OMAiFAFKCAA.
OrthoDBiPOG091H05DA.

Family and domain databases

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.
IPR016040. NAD(P)-bd_dom.
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.

C3KDC5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFLALGINH KTASVDVRER VAFTPEQLVE ALQQLCRLTD SREAAILSTC
60 70 80 90 100
NRSELYIEQE HLSADVVLRW LADYHHLDLD DLRASAYVHE DDAAVRHMMR
110 120 130 140 150
VASGLDSLVL GEPQILGQMK SAYAVAREAG TVGPLLGRLF QATFNSAKQV
160 170 180 190 200
RTDTAIGENP VSVAFAAVSL AKQIFSDLQR SQALLIGAGE TITLVARHLH
210 220 230 240 250
DLGVKRIVVA NRTLERASIL AEQFGAHAVL LADIPAELVR SDIVISSTAS
260 270 280 290 300
QLPILGKGAV ESALKLRKHK PIFMVDIAVP RDIEPEVGEL DDVYLYSVDD
310 320 330 340 350
LHEVVAENLK SRQGAAQAAE EMVSAGADDF MVRLRELAAV DVLKAYRQQG
360 370 380 390 400
ERLRDEELLK AQRLLANGSS AEDVLVQLAR GLTNKLLHAP SVQLKKLTAE
410 420
GRLDALAMAQ ELFALGEGAS DSSSDKKLQ
Length:429
Mass (Da):46,669
Last modified:June 16, 2009 - v1
Checksum:i959466EDB03B03C4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM181176 Genomic DNA. Translation: CAY47005.1.
RefSeqiWP_012722109.1. NC_012660.1.

Genome annotation databases

EnsemblBacteriaiCAY47005; CAY47005; PFLU_0737.
KEGGipfs:PFLU_0737.
PATRICifig|216595.4.peg.971.

Similar proteinsi

Entry informationi

Entry nameiHEM1_PSEFS
AccessioniPrimary (citable) accession number: C3KDC5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 16, 2009
Last modified: September 27, 2017
This is version 63 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

Documents

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