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Protein

Glutamyl-tRNA reductase

Gene

hemA

Organism
Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99)
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 sitei59 – 591NucleophileUniRule annotation
Sitei111 – 1111Important for activityUniRule annotation
Binding sitei121 – 1211SubstrateUniRule annotation
Binding sitei132 – 1321SubstrateUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi203 – 2086NADPUniRule 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

BioCyciHPYL85963:GJB9-232-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:jhp_0224
OrganismiHelicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99)
Taxonomic identifieri85963 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter
ProteomesiUP000000804 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 449449Glutamyl-tRNA reductasePRO_0000114033Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi85963.jhp0224.

Structurei

3D structure databases

ProteinModelPortaliQ9ZMJ5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 614Substrate bindingUniRule annotation
Regioni126 – 1283Substrate 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.
OMAiGAHSISM.
OrthoDBiEOG6MWNBM.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9ZMJ5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELETHLSKY FTLAFTHKSM SLEMREKLAI NSPIMLKELL QTIKTHCPNI
60 70 80 90 100
KECMVLSTCN RFEIYASLKH GANTHEQKSA LLKILAQNKK MSVSDLEKCV
110 120 130 140 150
LINTDESAVH HVFSVCSSLD SLVVGETQIT GQMKNAYKFA FEEKFCSKDL
160 170 180 190 200
TRLLHFAFKC AAKVRNLTGI SKQGVSISSV AVKEALSIFE KERIKDKKAL
210 220 230 240 250
VIGLGEMAQL VIKHLLNKQF EVLILGRNAA KFEDFVKELE EPKKVGFQNV
260 270 280 290 300
ENLNAYINEY ELLFCATSSP NFIVRNSMLK ETIFRRFWFD LAVPRNIEKP
310 320 330 340 350
TLNHIFLYSV DDLEPMVKEN VGNRQESRTK AYEIVGLATM EFYQWIQSLE
360 370 380 390 400
VEPLIKDLRE LARISAQKEL QKALKKRYVP KEYEGNIEKI LHNAFNTFLH
410 420 430 440
HPTIALKKNA QKEESDVLVG AIKNLFNLDK SNANHAQNLN LYKCEYYEE
Length:449
Mass (Da):51,613
Last modified:May 1, 1999 - v1
Checksum:i2BB93FFD34AC2C69
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001439 Genomic DNA. Translation: AAD05796.1.
PIRiC71959.
RefSeqiNP_222945.1. NC_000921.1.
WP_000418347.1. NC_000921.1.

Genome annotation databases

EnsemblBacteriaiAAD05796; AAD05796; jhp_0224.
KEGGihpj:jhp0224.
PATRICi20605089. VBIHelPyl98156_0255.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE001439 Genomic DNA. Translation: AAD05796.1.
PIRiC71959.
RefSeqiNP_222945.1. NC_000921.1.
WP_000418347.1. NC_000921.1.

3D structure databases

ProteinModelPortaliQ9ZMJ5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi85963.jhp0224.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD05796; AAD05796; jhp_0224.
KEGGihpj:jhp0224.
PATRICi20605089. VBIHelPyl98156_0255.

Phylogenomic databases

eggNOGiCOG0373.
KOiK02492.
OMAiGAHSISM.
OrthoDBiEOG6MWNBM.

Enzyme and pathway databases

UniPathwayiUPA00251; UER00316.
BioCyciHPYL85963:GJB9-232-MONOMER.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_00087. Glu_tRNA_reductase.
InterProiIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR018214. GluRdtase_CS.
IPR016040. NAD(P)-bd_dom.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFiPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMiSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsiTIGR01035. hemA. 1 hit.
PROSITEiPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: J99 / ATCC 700824.

Entry informationi

Entry nameiHEM1_HELPJ
AccessioniPrimary (citable) accession number: Q9ZMJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: May 27, 2015
This is version 106 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.