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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chlamydophila caviae (strain GPIC)
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

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

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Porphyrin biosynthesis

Keywords - Ligandi

NADP

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: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.
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

HAMAPiMF_00087. Glu_tRNA_reductase. 1 hit.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
[Graphical view]
PfamiPF05201. GlutR_N. 1 hit.
[Graphical view]
SUPFAMiSSF69742. SSF69742. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

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.
PATRICi20269038. VBIChlCav107360_0029.

Cross-referencesi

Sequence databases

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

3D structure databases

ProteinModelPortaliQ824W1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi227941.CCA00028.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAP04780; AAP04780; CCA_00028.
KEGGicca:CCA_00028.
PATRICi20269038. VBIChlCav107360_0029.

Phylogenomic databases

eggNOGiENOG4105C7E. Bacteria.
COG0373. LUCA.
KOiK02492.
OMAiCHRAELY.
OrthoDBiPOG091H05DA.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.

Family and domain databases

HAMAPiMF_00087. Glu_tRNA_reductase. 1 hit.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
[Graphical view]
PfamiPF05201. GlutR_N. 1 hit.
[Graphical view]
SUPFAMiSSF69742. SSF69742. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHEM1_CHLCV
AccessioniPrimary (citable) accession number: Q824W1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 2003
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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

Keywords - Technical termi

Complete proteome

Documents

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

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.