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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440)
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
Sitei99Important for activityUniRule annotation1
Binding sitei109SubstrateUniRule annotation1
Binding sitei120SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi190 – 195NADPUniRule 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:Strop_0356
OrganismiSalinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440)
Taxonomic identifieri369723 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicromonosporalesMicromonosporaceaeSalinispora
Proteomesi
  • UP000000235 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000754241 – 455Glutamyl-tRNA reductaseAdd BLAST455

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi369723.Strop_0356

Structurei

3D structure databases

ProteinModelPortaliA4X1U1
SMRiA4X1U1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni49 – 52Substrate bindingUniRule annotation4
Regioni114 – 116Substrate 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
HOGENOMiHOG000109649
KOiK02492
OMAiFAFKCAA
OrthoDBiPOG091H05DA

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
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

Sequencei

Sequence statusi: Complete.

A4X1U1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLLVVGASY RTAPVAALER LTVAPADLSR VLTRLVAQPY VSEAVLVSTC
60 70 80 90 100
NRVEVYAVVS GFHGGLGDIC AVLAESTGCQ PAALADHLYV HFDAAAVNHV
110 120 130 140 150
FRVAVGLDSM VVGEAQILGQ LRDAYHWASE AETVGRLLHE LMQQALRVGK
160 170 180 190 200
RAHSETGIDR AGQSVVTAAL GLATELLHSD LACRPALVVG AGAMGSLGVA
210 220 230 240 250
TLARLGAGPV SVTNRGVDRA IRLAESYGAT AVPIADLTAT LSTVDIVVAA
260 270 280 290 300
TAAPEAVLTR AVVTQALAGR NPSRGPLVLL DLAVPRDVEP GVADLPGVQV
310 320 330 340 350
IDIDRMAALV ADGPVAADAA AVEQIVAAEV DTFLTWLRGA DVAPTVAALR
360 370 380 390 400
GRADDVVAAE LGRLVHRRPD LTDEQRADVA RTVHRVVQRL LHQPTVRVRQ
410 420 430 440 450
LAAEPGGDQY TALLRELFDL EVPQTSAVGT VPDVVVPDVD PQLGGDAEAP

PTGGE
Length:455
Mass (Da):47,268
Last modified:May 29, 2007 - v1
Checksum:iE11D84256B38311B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000667 Genomic DNA Translation: ABP52841.1
RefSeqiWP_011904275.1, NC_009380.1

Genome annotation databases

EnsemblBacteriaiABP52841; ABP52841; Strop_0356
GeneIDi5056794
KEGGistp:Strop_0356
PATRICifig|369723.5.peg.367

Similar proteinsi

Entry informationi

Entry nameiHEM1_SALTO
AccessioniPrimary (citable) accession number: A4X1U1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 29, 2007
Last modified: March 28, 2018
This is version 80 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
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Main funding by: National Institutes of Health