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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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 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

BioCyciPAER208964:G1FZ6-4762-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:PA4666
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi

Organism-specific databases

PseudoCAPiPA4666

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001140581 – 422Glutamyl-tRNA reductaseAdd BLAST422

Proteomic databases

PaxDbiP42807

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi208964.PA4666

Structurei

3D structure databases

ProteinModelPortaliP42807
SMRiP42807
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
InParanoidiP42807
KOiK02492
OMAiFAFKCAA
PhylomeDBiP42807

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.

P42807-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFIALGINH KTASVAVRER VAFTPEQMVE ALQQLCRLTT SREAAILSTC
60 70 80 90 100
NRSELYLEID HPTADDVLAW LADYHRLTLD ELRACAYVHQ DEDAVRHMMR
110 120 130 140 150
VASGLDSMVL GEPQILGQMK SAYAVAREAG TVGPLLGRLF QATFSTAKTV
160 170 180 190 200
RTDTAIGENP VSVAFAAVSL AKQIFSDLHR SQALLIGAGE TITLVARHLF
210 220 230 240 250
EQGVKRIVVA NRTLERASLL AEQFGAHAVL LSEIPEELAN SDIVISSTAS
260 270 280 290 300
QLPILGKGAV ERALKQRKHK PMFMVDIAVP RDIEPEVGEL DDVYLYSVDD
310 320 330 340 350
LHEVVAENLK SRQGAAQAAE ELVGSGVAEF MQRLRELAAV DVLRAYRQQA
360 370 380 390 400
ERLRDEELGK AQRQLANGAD PAEVMAQLAR GLTNKLLHAP SVQMKKMSAE
410 420
GRIDALALAQ ELFALDEGAP RH
Length:422
Mass (Da):46,124
Last modified:December 8, 2000 - v3
Checksum:i33EA54A65BA94787
GO

Sequence cautioni

The sequence CAA57574 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti59I → V in CAA57574 (PubMed:7883699).Curated1
Sequence conflicti153 – 155DTA → ETD in CAA57574 (PubMed:7883699).Curated3
Sequence conflicti314G → A in CAA57574 (PubMed:7883699).Curated1
Sequence conflicti343L → V in CAA57574 (PubMed:7883699).Curated1
Sequence conflicti418G → C in CAA57574 (PubMed:7883699).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82071 Genomic DNA Translation: CAA57574.1 Different initiation.
AE004091 Genomic DNA Translation: AAG08053.1
PIRiC83063
RefSeqiNP_253355.1, NC_002516.2
WP_003095001.1, NC_002516.2

Genome annotation databases

EnsemblBacteriaiAAG08053; AAG08053; PA4666
GeneIDi881361
KEGGipae:PA4666
PATRICifig|208964.12.peg.4888

Entry informationi

Entry nameiHEM1_PSEAE
AccessioniPrimary (citable) accession number: P42807
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 8, 2000
Last modified: March 28, 2018
This is version 136 of the entry and version 3 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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