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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).1 Publication

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 (By similarity).By similarity

Catalytic activityi

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH.1 Publication

pH dependencei

Optimum pH is 7.0.1 Publication

Temperature dependencei

Optimum temperature is 65 degrees Celsius.1 Publication

Pathwayi: protoporphyrin-IX biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 5-aminolevulinate from L-glutamyl-tRNA(Glu).
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 sitei46NucleophileBy similarity1
Sitei78Important for activityBy similarity1
Binding sitei88SubstrateBy similarity1
Binding sitei99SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi168 – 173NADPBy similarity6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPorphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

BioCyciMMAR79929:G1GML-1375-MONOMER
UniPathwayiUPA00251; UER00316

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamyl-tRNA reductase (EC:1.2.1.70)
Short name:
GluTR
Gene namesi
Name:hemA
Ordered Locus Names:MTBMA_c13940
OrganismiMethanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri79929 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000000345 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001141061 – 398Glutamyl-tRNA reductaseAdd BLAST398

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi79929.MTBMA_c13940

Structurei

3D structure databases

ProteinModelPortaliP42809
SMRiP42809
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni45 – 48Substrate bindingBy similarity4
Regioni93 – 95Substrate bindingBy similarity3

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 (By similarity).By similarity

Sequence similaritiesi

Belongs to the glutamyl-tRNA reductase family.Curated

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.

P42809-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILNIRLDHK TSDVKTMETA SGRIEEIVGE LEALGAVTEK VPLMTCNRVE
60 70 80 90 100
YYLHVTGVPP EFDFNGFTVE KDEDALLHLL RLASGLESMI IGEDQILGQI
110 120 130 140 150
KAARLQALRE GTCGPLLDMV FTKAVHVGQT VRRKTKINRG SVSIGSAAVD
160 170 180 190 200
LAESIHGDLK CKKVLVIGAG KMGTLVARAL AEKHLKAIMV ANRTYERAYQ
210 220 230 240 250
LACELGGDAI HFDRLNRALR DADVVISATG SPHYILTRER VMDAVPPERR
260 270 280 290 300
SSIVMVDIAN PRDIEESVRE LGVRLFTIDD LRGVAEENRK RREAEAREAE
310 320 330 340 350
GIVRAELELL LRAMKHREVE PLLAEIRGRM ESLRQREAGK AIKKIENSKD
360 370 380 390
PERVVEGLTR SIVDKIFHDI ALKIRDAAER DDREFLRMCS ELFDCDES
Length:398
Mass (Da):44,536
Last modified:November 1, 1995 - v1
Checksum:i7A2C457D9E48CB67
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X83691 Genomic DNA Translation: CAA58664.1
CP001710 Genomic DNA Translation: ADL58981.1
PIRiS51136
RefSeqiWP_013296193.1, NC_014408.1

Genome annotation databases

EnsemblBacteriaiADL58981; ADL58981; MTBMA_c13940
GeneIDi9705103
KEGGimmg:MTBMA_c13940
PATRICifig|79929.8.peg.1358

Similar proteinsi

Entry informationi

Entry nameiHEM1_METTM
AccessioniPrimary (citable) accession number: P42809
Secondary accession number(s): D9PXN3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: March 28, 2018
This is version 118 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

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