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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chlamydia muridarum (strain MoPn / Nigg)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-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 sitei61NucleophileUniRule annotation1
Sitei100Important for activityUniRule annotation1
Binding sitei110SubstrateUniRule annotation1
Binding sitei121SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi189 – 194NADPUniRule 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:TC_0033
OrganismiChlamydia muridarum (strain MoPn / Nigg)
Taxonomic identifieri243161 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
Proteomesi
  • UP000000800 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001140051 – 333Glutamyl-tRNA reductaseAdd BLAST333

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi243161.CmurN_010100000165.

Structurei

3D structure databases

ProteinModelPortaliQ9PLR2.
SMRiQ9PLR2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni60 – 63Substrate bindingUniRule annotation4
Regioni115 – 117Substrate 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.
KOiK02492.
OMAiCHRAELY.

Family and domain databases

HAMAPiMF_00087. Glu_tRNA_reductase. 1 hit.
InterProiView protein in InterPro
IPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
PfamiView protein in Pfam
PF05201. GlutR_N. 1 hit.
SUPFAMiSSF69742. SSF69742. 1 hit.
PROSITEiView protein in PROSITE
PS00747. GLUTR. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9PLR2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVREGEEHID EEFSLGVIGV SYRETALQQR EQVLQFLQQA QLSFYPKFPQ
60 70 80 90 100
EEGRSVLLST CHRVELYGMA TEAIFSTLEK EIREMGAIPY FYRNQDCFSH
110 120 130 140 150
LFCVVGGMDS LVLGETEIQG QVKRAYLQAI EEQKLAFALH FLFQKALKEG
160 170 180 190 200
KVFRTKRSSP STEITIPAFV QHELQKQKMA RSASLLFMGY SEINRSVAYY
210 220 230 240 250
LQKQGFSRIT FCSRQPLSLR SMDQVLREEV CFQDPYHVIF LGSSELRHAF
260 270 280 290 300
PRSLWEGVWD FPGRLVFDFA VPRALPVQPA CRDRYIDMEQ ISDWLRQHQK
310 320 330
EVFPLQLDSL REVGYRYWES LNRRLARRRY ASV
Length:333
Mass (Da):39,016
Last modified:October 1, 2000 - v1
Checksum:i81D9B761ECC8A986
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE002160 Genomic DNA. Translation: AAF38924.1.
PIRiE81748.
RefSeqiWP_010229174.1. NZ_ACOV01000001.1.

Genome annotation databases

EnsemblBacteriaiAAF38924; AAF38924; TC_0033.
GeneIDi1245558.
KEGGicmu:TC_0033.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiHEM1_CHLMU
AccessioniPrimary (citable) accession number: Q9PLR2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: June 7, 2017
This is version 100 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

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families