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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis)
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 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:CTLon_0031
OrganismiChlamydia trachomatis serovar L2b (strain UCH-1/proctitis)
Taxonomic identifieri471473 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000931261 – 335Glutamyl-tRNA reductaseAdd BLAST335

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliB0BAB7
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

HOGENOMiHOG000110628
KOiK02492
OMAiCHRAELY

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
IPR015895 4pyrrol_synth_GluRdtase_N
IPR018214 GluRdtase_CS
IPR036343 GluRdtase_N_sf
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.

B0BAB7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVREGEERIG NRVLLGVIGV SYRETTLQQR EQVLHILQQA QGSFRPEVFQ
60 70 80 90 100
EERDYVLLAT CHRVELYSVA PAELFDSLAQ EIKLLGVSPY FYRNQDCFAH
110 120 130 140 150
LFCVAGGLDS LVLGETEIQG QVKRAYLQAA REQKLSFALH FLFQKALKEG
160 170 180 190 200
KVFRAKGGAP YAAITIPILV DQELRRRQID KKASLLFIGY SEINRSVAYH
210 220 230 240 250
LRRQGFSCIT FCSRQQLPTL SMRQVVREEL CFQDPYRVVF LGSLELQYAL
260 270 280 290 300
PHSLWESIWD IPDRIVFDFA VPRALPSHTV FPHRYMDMDQ ISDWLREHRK
310 320 330
EVNSAHLDSL REVAYRYWNS LNQRLERHDC VGANA
Length:335
Mass (Da):38,868
Last modified:February 26, 2008 - v1
Checksum:i3BAE3959FB93A1A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AM884177 Genomic DNA Translation: CAP06429.1
RefSeqiWP_009873277.1, NC_010280.2

Genome annotation databases

EnsemblBacteriaiCAP06429; CAP06429; CTLon_0031
KEGGictl:CTLon_0031

Similar proteinsi

Entry informationi

Entry nameiHEM1_CHLTB
AccessioniPrimary (citable) accession number: B0BAB7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 26, 2008
Last modified: April 25, 2018
This is version 62 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health