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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)
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 sitei51NucleophileUniRule annotation1
Sitei93Important for activityUniRule annotation1
Binding sitei103SubstrateUniRule annotation1
Binding sitei114SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi182 – 187NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPorphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

BioCyciHWAL362976:G1G1J-2430-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:HQ_3336A
OrganismiHaloquadratum walsbyi (strain DSM 16790 / HBSQ001)
Taxonomic identifieri362976 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHaloferacalesHaloferacaceaeHaloquadratum
Proteomesi
  • UP000001975 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003350881 – 454Glutamyl-tRNA reductaseAdd BLAST454

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi362976.HQ3336A

Structurei

3D structure databases

ProteinModelPortaliQ18F28
SMRiQ18F28
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni50 – 53Substrate bindingUniRule annotation4
Regioni108 – 110Substrate 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

eggNOGiarCOG01036 Archaea
COG0373 LUCA
HOGENOMiHOG000109651
KOiK02492
OMAiFAFKCAA
OrthoDBiPOG093Z06M3

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.

Q18F28-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTGVICGVR VSHNRASVEE IELAGERDSR TIMETLLTRD GITESFAIQT
60 70 80 90 100
CNRSEAYVVA DGAVAGRRAL ASFAPDVRDG AVVDMSHEES LRHLLRVATG
110 120 130 140 150
LESLVLGEDQ ILGQFKRAIE VARGIGALGP MLEAGVTKAI HVGERARSET
160 170 180 190 200
SINEGAVSIG SAAVRLAGQS VGLNGRKALV IGAGEMGSLV AESLASTNIS
210 220 230 240 250
EVVIANRTIE NAESIAETIN SPAYAVSLDS LTEVITEASI IMTATGYGKY
260 270 280 290 300
LIEPTDIDGA GETFIIDLAQ PRNVHPATAD IENAIVQDID ALESITKETE
310 320 330 340 350
ASRQAAAREV DAMIDEEFDR LLESYKRQRA DEAISEMYEA AEHVKRREVE
360 370 380 390 400
TALEKLEKQG TLTDNQRETI SSMADTLINQ LLAAPTKSLR DAAAEDDWTT
410 420 430 440 450
IQTAMTLFDP NFGGDTPQPD RPDDIPRAAE RGDISGDDLP DDVPNHIAEK

VSDG
Length:454
Mass (Da):48,625
Last modified:July 25, 2006 - v1
Checksum:i2D20D329DCA6FDDC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM180088 Genomic DNA Translation: CAJ53433.1
RefSeqiWP_011572535.1, NC_008212.1

Genome annotation databases

EnsemblBacteriaiCAJ53433; CAJ53433; HQ_3336A
GeneIDi4194102
KEGGihwa:HQ_3336A

Similar proteinsi

Entry informationi

Entry nameiHEM1_HALWD
AccessioniPrimary (citable) accession number: Q18F28
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 25, 2006
Last modified: March 28, 2018
This is version 94 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