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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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei51 – 511NucleophileUniRule annotation
Sitei92 – 921Important for activityUniRule annotation
Binding sitei102 – 1021SubstrateUniRule annotation
Binding sitei113 – 1131SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi181 – 1866NADPUniRule annotation

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

BioCyciCCAV227941:GH8L-30-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 groupChlamydophila
ProteomesiUP000002193 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 338338Glutamyl-tRNA reductasePRO_0000114004Add
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Regioni50 – 534Substrate bindingUniRule annotation
Regioni107 – 1093Substrate bindingUniRule annotation

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

eggNOGiCOG0373.
KOiK02492.
OMAiCHRAELY.
OrthoDBiEOG6MWNBM.

Family and domain databases

HAMAPiMF_00087. Glu_tRNA_reductase.
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.
RefSeqiNP_828902.1. NC_003361.3.
WP_011006001.1. NC_003361.3.

Genome annotation databases

EnsemblBacteriaiAAP04780; AAP04780; CCA_00028.
KEGGicca:CCA00028.
PATRICi20269038. VBIChlCav107360_0029.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015925 Genomic DNA. Translation: AAP04780.1.
RefSeqiNP_828902.1. NC_003361.3.
WP_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:CCA00028.
PATRICi20269038. VBIChlCav107360_0029.

Phylogenomic databases

eggNOGiCOG0373.
KOiK02492.
OMAiCHRAELY.
OrthoDBiEOG6MWNBM.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.
BioCyciCCAV227941:GH8L-30-MONOMER.

Family and domain databases

HAMAPiMF_00087. Glu_tRNA_reductase.
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...

Publicationsi

  1. "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC): examining the role of niche-specific genes in the evolution of the Chlamydiaceae."
    Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T., Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A., Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O., Salzberg S.L., Hsia R.-C., McClarty G.
    , Rank R.G., Bavoil P.M., Fraser C.M.
    Nucleic Acids Res. 31:2134-2147(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: GPIC.

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: April 1, 2015
This is version 83 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

External Data

Dasty 3

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 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.