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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Chlamydia trachomatis (strain D/UW-3/Cx)
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 sitei61NucleophileUniRule annotation1
Sitei100Important for activityUniRule annotation1
Binding sitei110SubstrateUniRule annotation1
Binding sitei121SubstrateUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi189 – 194NADPUniRule 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:CT_662
OrganismiChlamydia trachomatis (strain D/UW-3/Cx)
Taxonomic identifieri272561 [NCBI]
Taxonomic lineageiBacteriaChlamydiaeChlamydialesChlamydiaceaeChlamydia/Chlamydophila groupChlamydia
Proteomesi
  • UP000000431 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001140081 – 335Glutamyl-tRNA reductaseAdd BLAST335

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi272561.CT662.

Structurei

3D structure databases

ProteinModelPortaliO84669.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni60 – 63Substrate bindingUniRule annotation4
Regioni115 – 117Substrate 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.
InParanoidiO84669.
KOiK02492.
OMAiCHRAELY.

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.

O84669-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVREGEERIG NRVSLGVIGV SYRETTLQQR EQVLHILQQA QGSFRPEVFQ
60 70 80 90 100
EERDYVLLAT CHRVELYSVA PAELFDSLAQ EIELLGVSPY FYRNQDCFAH
110 120 130 140 150
LFCVAGGLDS LVLGETEIQG QVKRAYLQAA REQKLSFALH FLFQKALKEG
160 170 180 190 200
KVFRAKGGAP YAEITIPILV DQELRRRQID KKASLLFIGY SEINRSVAYH
210 220 230 240 250
LQRQGFSCIT FCSRQQLPTL SMRQVVREEL CFQDPYRVVF LGSSELQYAL
260 270 280 290 300
PHSLWESIWD IPDRIVFDFA VPRALPSHTV FPHRYVDMDQ ISDWLREHRK
310 320 330
EVNSAHLHSL REVAYRYWNS LNQRLERRDC VGANA
Length:335
Mass (Da):38,855
Last modified:May 30, 2000 - v2
Checksum:iA7F799AFB3FBE61F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001273 Genomic DNA. Translation: AAC68257.2.
PIRiH71487.
RefSeqiNP_220181.1. NC_000117.1.
WP_010725294.1. NC_000117.1.

Genome annotation databases

EnsemblBacteriaiAAC68257; AAC68257; CT_662.
GeneIDi884447.
KEGGictr:CT_662.
PATRICi20380972. VBIChlTra43535_0728.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001273 Genomic DNA. Translation: AAC68257.2.
PIRiH71487.
RefSeqiNP_220181.1. NC_000117.1.
WP_010725294.1. NC_000117.1.

3D structure databases

ProteinModelPortaliO84669.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272561.CT662.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC68257; AAC68257; CT_662.
GeneIDi884447.
KEGGictr:CT_662.
PATRICi20380972. VBIChlTra43535_0728.

Phylogenomic databases

eggNOGiENOG4105C7E. Bacteria.
COG0373. LUCA.
InParanoidiO84669.
KOiK02492.
OMAiCHRAELY.

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_CHLTR
AccessioniPrimary (citable) accession number: O84669
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: September 7, 2016
This is version 97 of the entry and version 2 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, Reference 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.