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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chlamydophila caviae (strain GPIC)
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 sitei51NucleophileUniRule annotation1
Sitei92Important for activityUniRule annotation1
Binding sitei102SubstrateUniRule annotation1
Binding sitei113SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi181 – 186NADPUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processPorphyrin biosynthesis
LigandNADP

Enzyme and pathway databases

BioCyciCCAV227941:G1G03-31-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:CCA_00028
OrganismiChlamydophila caviae (strain GPIC)
Taxonomic identifieri227941 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
Proteomesi
  • UP000002193 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001140041 – 338Glutamyl-tRNA reductaseAdd BLAST338

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi227941.CCA00028

Structurei

3D structure databases

ProteinModelPortaliQ824W1
SMRiQ824W1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni50 – 53Substrate bindingUniRule annotation4
Regioni107 – 109Substrate 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
OrthoDBiPOG091H05DA

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.

Q824W1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLGVVGISY REAALKEREA AINILKDFEA NTLFSQRFFG GEGSFVLLLT
60 70 80 90 100
CHRAEIYYFS KSNHNVQSEL LSRISALGAR PYCYQGLACF THLFTVTSGM
110 120 130 140 150
DSLISGETEI QGQVKRAYIK AKTDRELPFA LHFLFQKALK EGKDFRSQVS
160 170 180 190 200
LSHPVVTIES VVEQTLDLHG KSTKDKLLFI GYSDINRKVA NGLSAKGYRN
210 220 230 240 250
LIFCSRKNIS IPYATVARSQ LSFREPYDVI FFGSSESAKD FPGLSLENLA
260 270 280 290 300
SISNRVIFDF NVPRTFTLME RPKDIVCLDM DFISEQVQKK LQISKQCTNK
310 320 330
EKPFLALAAR KQWEVYEKKC SHISSSQLQT SRPKLLIL
Length:338
Mass (Da):38,246
Last modified:June 1, 2003 - v1
Checksum:i74BD254818939641
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015925 Genomic DNA Translation: AAP04780.1
RefSeqiWP_011006001.1, NC_003361.3

Genome annotation databases

EnsemblBacteriaiAAP04780; AAP04780; CCA_00028
KEGGicca:CCA_00028

Similar proteinsi

Entry informationi

Entry nameiHEM1_CHLCV
AccessioniPrimary (citable) accession number: Q824W1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: March 28, 2018
This is version 95 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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