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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)
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 sitei39NucleophileUniRule annotation1
Sitei72Important for activityUniRule annotation1
Binding sitei82SubstrateUniRule annotation1
Binding sitei93SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi161 – 166NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPorphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

BioCyciMAEO419665:G1G9A-51-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:Maeo_0052
OrganismiMethanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)
Taxonomic identifieri419665 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanococcaceaeMethanococcus
Proteomesi
  • UP000001106 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000046351 – 383Glutamyl-tRNA reductaseAdd BLAST383

Proteomic databases

PRIDEiA6UT22

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi419665.Maeo_0052

Structurei

3D structure databases

ProteinModelPortaliA6UT22
SMRiA6UT22
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni38 – 41Substrate bindingUniRule annotation4
Regioni87 – 89Substrate 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
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.

A6UT22-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLFRADYNN YAVSELQKLR FDEDEFYKKY DNCVLVQTCN RIEIYFDKNA
60 70 80 90 100
KIIDINEFAE FEMIKSNNAI KHLLRTASGL NSMIVGEDQI IGQIKNSHRK
110 120 130 140 150
AKELKKTTKY LDTIFLKAIH TGQKVRNNTK INKGCVSIGS AAVQLAEKTV
160 170 180 190 200
GLNNKNILVV GAGEIATLVA KALIEKNIRA IVVSNRTYER AELLAKKLNG
210 220 230 240 250
MAVHFDKLGE AINYNDIIIC ATGAPHAIID KDRLKNIKGY KVLIDIANPR
260 270 280 290 300
DVSDDVMELP NIKLYTIDDL KMVSEENLKK RKDEIPRVEK IIEEELSVLT
310 320 330 340 350
KQLRKLKFEN TIKNYDLYIE NLRKREMNKA LNMIENGKDP TVVLEKFSKV
360 370 380
FANKLISDFV NIVNDDTIGD IERVVNKLNK NKI
Length:383
Mass (Da):43,752
Last modified:August 21, 2007 - v1
Checksum:i24EA373469361A60
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000743 Genomic DNA Translation: ABR55644.1
RefSeqiWP_011972776.1, NC_009635.1

Genome annotation databases

EnsemblBacteriaiABR55644; ABR55644; Maeo_0052
GeneIDi5326829
KEGGimae:Maeo_0052

Similar proteinsi

Entry informationi

Entry nameiHEM1_META3
AccessioniPrimary (citable) accession number: A6UT22
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: May 23, 2018
This is version 75 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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