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Reviewed, UniProtKB/Swiss-Prot Q9PHX2 (HEM1_CAMJE)

Last modified June 16, 2009. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Glutamyl-tRNA reductase
      Short name=GluTR
    EC=1.2.1.70
Gene names
Name: hemA
Ordered Locus Names: Cj0542
OrganismCampylobacter jejuni [Complete proteome] [HAMAP]
Taxonomic identifier197 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

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Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) By similarity.

Catalytic activity

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP MF_00087

Pathway

Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP MF_00087

Subunit structure

Homodimer By similarity.

Domain

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 By similarity.

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 By similarity.

Sequence similarities

Belongs to the glutamyl-tRNA reductase family.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

flaGQ0PAW91EBI-1192549,EBI-1191365
fliLQ0P8K61EBI-1192549,EBI-1191158

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Glutamyl-tRNA reductase HAMAP MF_00087
PRO_0000114002

Regions

Nucleotide binding186 – 1916NADP By similarity
Region49 – 524Substrate binding By similarity
Region112 – 1143Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site1071Substrate By similarity
Binding site1181Substrate By similarity
Site971Important for activity By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q9PHX2-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 5BB55DF90CBA3F22

FASTA43248,697
        10         20         30         40         50         60 
MYYCISFTHK NTDIALREKL SFSNEAKKGE FLKIISTHEN IEECLVISTC NRVEIVAFVK 

        70         80         90        100        110        120 
MACAEFIVKS LALLCDVDKD ILLEKADIFE DSGAIHHLFS VASSLDSLVV GETQIAGQLK 

       130        140        150        160        170        180 
DAFAFAVKNN FCGVHLSRAV HSAFKCAAKV RNETQISKNS ISVASVAVAK AKELADLTQK 

       190        200        210        220        230        240 
KAVVIGAGEM GELAAKHLIA AGAKVIILNR DLQKAKDLCE RLGVLSEYDS LENLKKYLNQ 

       250        260        270        280        290        300 
YEFFFSATNA PNAIITNSLI EELSYKRYFF DIAVPRDIDI NENENISVFA VDDLEIVVQK 

       310        320        330        340        350        360 
NLALREQEAR MAYGIIGRET SEFFRYLNDL ALMPIIKAIR LQAKEYADKQ LEIALKKGYL 

       370        380        390        400        410        420 
KKSDKEEARK LIHQVFKAFL HTPTVNLKHL QGKMQSDTVI NAMRYVFDLQ NNLEGLNQYK 

       430 
CEFDMENNDE IY

« Hide

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References

[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed: 10688204] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168 / Serotype O:2.

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Cross-references

Sequence databases

AL111168 Genomic DNA. Translation: CAL34688.1.
PIRF81400.
RefSeqYP_002343973.1.

3D structure databases

HSSPHSSP built from PDB template 1GPJ based on UniProtKB Q9UXR8.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9PHX2. 80 interactions.

Genome annotation databases

GeneID904868.
GenomeReviewsGene locus Cj0542 in contig AL111168_GR.
KEGGcje:Cj0542.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAQ9PHX2. GPILNRL.

Enzyme and pathway databases

BioCycCJEJ192222:CJ0542-MON.
BRENDA1.2.1.70. 255835.

Family and domain databases

HAMAPMF_00087.
[Tree]
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_C.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR018214. pyrrol_synth_GluRdtase_CS.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
TIGRFAMsTIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameHEM1_CAMJE
AccessionPrimary (citable) accession number: Q9PHX2
Secondary accession number(s): Q0PAX4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 59 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents