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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Pseudomonas stutzeri (strain A1501)
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:PST_3183
OrganismiPseudomonas stutzeri (strain A1501)
Taxonomic identifieri379731 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000000233 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000046751 – 422Glutamyl-tRNA reductaseAdd BLAST422

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi379731.PST_3183.

Structurei

3D structure databases

ProteinModelPortaliA4VPC0.
SMRiA4VPC0.
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.
HOGENOMiHOG000109650.
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.

A4VPC0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFLALGINH KTASVDVRER VAFTPDQMVE ALRQLCRVTP TREAAILSTC
60 70 80 90 100
NRSELYLQQD EVEAEAVLAW LASYHRLSLD ELKACAYVHV DDQAVRHMMR
110 120 130 140 150
VASGLDSLVL GEPQILGQMK SAYAVAREAG SVGPLLGRLF QATFSTAKTV
160 170 180 190 200
RTDTAIGENP VSVAFAAVSL ARQIFSNLQR SQALLIGAGE TITLVARHLH
210 220 230 240 250
EQGVKRIVVA NRTLERASAL AAELGAHAIL LADIPDELHN SDIVISSTAS
260 270 280 290 300
QLPILGKGAV EQALKRRKHK PMFMVDIAVP RDIESQVGEL DDVYLYTVDD
310 320 330 340 350
LHEVVAENLK SRQGAAQAAE ELVAAGTEDF MQRLRELAAV DVLKAYRQHA
360 370 380 390 400
ERIRDDELSK AQRLLANGAS AEDALAQLAR GLTNKLLHAP SVQLKKLSAE
410 420
GRVEALSMAQ ELFALHEGTE KP
Length:422
Mass (Da):45,950
Last modified:May 29, 2007 - v1
Checksum:i6964D8FB044765E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000304 Genomic DNA. Translation: ABP80821.1.
RefSeqiWP_011914266.1. NC_009434.1.

Genome annotation databases

EnsemblBacteriaiABP80821; ABP80821; PST_3183.
KEGGipsa:PST_3183.

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.

Entry informationi

Entry nameiHEM1_PSEU5
AccessioniPrimary (citable) accession number: A4VPC0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 29, 2007
Last modified: July 5, 2017
This is version 74 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