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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chlamydia pneumoniae (Chlamydophila pneumoniae)
Status
Unreviewed-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 annotationSAAS 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 annotationSAAS annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA), Glutamyl-tRNA reductase (hemA)
  2. Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), Glutamate-1-semialdehyde 2,1-aminomutase (hemL), 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 functionOxidoreductaseUniRule annotationSAAS annotationImported
Biological processPorphyrin biosynthesisUniRule annotationSAAS annotation
LigandNADPUniRule annotationSAAS annotation

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
ORF Names:BN1224_GiD_A_07440Imported, BN1224_Panola_K_00400Imported, BN1224_U1271_C_05740Imported, BN1224_UZG1_B_00400Imported, CWL029c_E_00390Imported
OrganismiChlamydia pneumoniae (Chlamydophila pneumoniae)Imported
Taxonomic identifieri83558 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA0A0F7WJV1
SMRiA0A0F7WJV1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini6 – 147GlutR_NInterPro annotationAdd BLAST142

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

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.

A0A0F7WJV1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVLGVVGISY REAALKERER AIQYLQSFEK NLFLAQRFLG KGGAFIPLLT
60 70 80 90 100
CHRAELYYYS ESPEIAQAAL LSELTSQGIR PYRHRGLSCF THLFQVTSGI
110 120 130 140 150
DSLIFGETEI QGQVKRAYLK GSKERELPFD LHFLFQKALK EGKEYRSRIG
160 170 180 190 200
FPDHQVTIES VVQEILLSYD KSIYTNFLFV GYSDINRKVA AYLYQHGYHR
210 220 230 240 250
ITFCSRQQVT APYRTLSRET LSFRQPYDVI FFGSSESASQ FSDLSCESLA
260 270 280 290 300
SIPKRIVFDF NVPRTFLWKE TPTGFVYLDI DFISECVQKR LQCTKEGVNK
310 320 330
AKLLLTCAAK KQWEIYEKKS SHITQRQISS PRIPSVLSY
Length:339
Mass (Da):39,104
Last modified:July 22, 2015 - v1
Checksum:i814E823518D6B157
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
LN847005 Genomic DNA Translation: CRI40615.1
LN847008 Genomic DNA Translation: CRI41743.1
LN847236 Genomic DNA Translation: CRI47341.1
LN847244 Genomic DNA Translation: CRI49634.1
LN847246 Genomic DNA Translation: CRI51891.1
RefSeqiWP_010883352.1, NZ_LN847221.1

Genome annotation databases

PATRICifig|83558.18.peg.760

Similar proteinsi

Entry informationi

Entry nameiA0A0F7WJV1_CHLPN
AccessioniPrimary (citable) accession number: A0A0F7WJV1
Entry historyiIntegrated into UniProtKB/TrEMBL: July 22, 2015
Last sequence update: July 22, 2015
Last modified: March 28, 2018
This is version 21 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

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