Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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 sitei53NucleophileUniRule annotation1
Sitei94Important for activityUniRule annotation1
Binding sitei104SubstrateUniRule annotation1
Binding sitei115SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi183 – 188NADPUniRule 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_PB1_B_07320Imported
OrganismiChlamydia pneumoniae (Chlamydophila pneumoniae)Imported
Taxonomic identifieri83558 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni52 – 55Substrate bindingUniRule annotation4
Regioni109 – 111Substrate 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

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.

A0A0F7XE38-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLMVLGVVGI SYREAALKER ERAIQYLQSF EKNLFLAQRF LGKGGAFIPL
60 70 80 90 100
LTCHRAELYY YSESPEIAQA ALLSELTSQG IRPYRHRGLS CFTHLFQVTS
110 120 130 140 150
GIDSLIFGET EIQGQVKRAY LKGSKERELP FDLHFLFQKA LKEGKEYRSR
160 170 180 190 200
IGFPDHQVTI ESVVQEILLS YDKSIYTNFL FVGYSDINRK VAAYLYQHGY
210 220 230 240 250
HRITFCSRQQ VTAPYRTLSR ETLSFRQPYD VIFFGSSESD SQFSDLSCES
260 270 280 290 300
LASIPKRIVF DFNVPRTFLW KETPTGFVYL DIDFISECVQ KRLQCTKEGV
310 320 330 340
NKAKLLLTCA AKKQWEIYEK KSSHITQRQI SSPRIPSVLS Y
Length:341
Mass (Da):39,392
Last modified:July 22, 2015 - v1
Checksum:iDDE15C40FCEA8936
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
LN847240 Genomic DNA Translation: CRI50763.1

Genome annotation databases

PATRICifig|83558.13.peg.756

Similar proteinsi

Entry informationi

Entry nameiA0A0F7XE38_CHLPN
AccessioniPrimary (citable) accession number: A0A0F7XE38
Entry historyiIntegrated into UniProtKB/TrEMBL: July 22, 2015
Last sequence update: July 22, 2015
Last modified: March 28, 2018
This is version 17 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health