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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
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
Sitei76Important for activityUniRule annotation1
Binding sitei86SubstrateUniRule annotation1
Binding sitei97SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi165 – 170NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPorphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

BioCyciMJAN243232:G1GKE-153-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:MJ0143
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001141011 – 392Glutamyl-tRNA reductaseAdd BLAST392

Proteomic databases

PRIDEiQ60172

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi243232.MJ_0143

Structurei

3D structure databases

ProteinModelPortaliQ60172
SMRiQ60172
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni38 – 41Substrate bindingUniRule annotation4
Regioni91 – 93Substrate 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
InParanoidiQ60172
KOiK02492
OMAiMANLVIK
OrthoDBiPOG093Z06M3
PhylomeDBiQ60172

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.

Q60172-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIILKADYKK YNVSELEKLR MDEEKFYETF DNAILLQTCN RVEIIFDADS
60 70 80 90 100
LEEIKGIENI DLEKFDILFG DKAIEHLFRV ACGLESMIVG EDQILGQLKN
110 120 130 140 150
AYLKAKEKGR ISKKLEKIIL KAIHTGQRAR VETKINEGGV SIGSAAVELA
160 170 180 190 200
EKIFGLEGKN VLLIGAGEMA NLVIKALKEK NIKAIIVANR TYEKAEKLAK
210 220 230 240 250
ELGGMAIKFD KLEEALRYAD IVISATGAPH PILNKERLKN AGKTIIIDIA
260 270 280 290 300
NPRDTTDDIR ELPDIFLFTI DDLRLVAEEN LKKRKEEIPK VEMIICEELE
310 320 330 340 350
RLKEFLDKMR FETAIKELGQ YIENVRKKEV EKAKKILKNK NKPVEEVLED
360 370 380 390
FSKALCKRII YDIIKIFENV EDKEVFECLA KEFKKLGNKN KN
Length:392
Mass (Da):44,847
Last modified:November 1, 1997 - v1
Checksum:i952E1CFDCDA3874C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA Translation: AAB98126.1
PIRiH64317
RefSeqiWP_010869638.1, NC_000909.1

Genome annotation databases

EnsemblBacteriaiAAB98126; AAB98126; MJ_0143
GeneIDi1450987
KEGGimja:MJ_0143

Similar proteinsi

Entry informationi

Entry nameiHEM1_METJA
AccessioniPrimary (citable) accession number: Q60172
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: March 28, 2018
This is version 125 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