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Reviewed, UniProtKB/Swiss-Prot Q6F8J3 (HEM1_ACIAD)

Last modified February 9, 2010. Version 45. 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 · 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: ACIAD2900
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter

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Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) By similarity. HAMAP MF_00087

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. HAMAP MF_00087

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. HAMAP MF_00087

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. HAMAP MF_00087

Sequence similarities

Belongs to the glutamyl-tRNA reductase family.

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Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

porphyrin biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular functionNADP or NADPH binding

Inferred from electronic annotation. Source: InterPro

glutamyl-tRNA reductase activity

Inferred from electronic annotation. Source: HAMAP

shikimate 5-dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431Glutamyl-tRNA reductase HAMAP MF_00087
PRO_0000113985

Regions

Nucleotide binding185 – 1906NADP By similarity
Region49 – 524Substrate binding By similarity
Region110 – 1123Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site1051Substrate By similarity
Binding site1161Substrate By similarity
Site951Important for activity By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q6F8J3-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: 26204FE6C6D7632E

FASTA43148,658
        10         20         30         40         50         60 
MSFFALGVNH QTASVELREQ VAFNAERLKD LLAQQRNHAH LNDMVVVSTC NRTEVYAMTE 

        70         80         90        100        110        120 
HADILLNWLA QTNGIDIKQL LHHVYRYEDA QAVTHLMRVA SGLDSLMLGE PQILGQVKSA 

       130        140        150        160        170        180 
LALSKESHTV SRDLNRIFEY AFYAAKRVRS ETAVGSHAVS MGYAVAQLAL QVFSNPEKLT 

       190        200        210        220        230        240 
VMMVAAGEMN TLVAKHLAEM GVAKVIICNR SRERAESLAQ EIAHQVEVEI IGFDQLAANL 

       250        260        270        280        290        300 
HRADVVSSCT GSLHQVIFYQ DVKAALKKRR YNQMLLVDLA VPRDIDSKVE TLDGVYLYGV 

       310        320        330        340        350        360 
DDLQSVIDEN LAQRRQAAVE AEVMVSQLAS QLLTHQKIQQ AGSTIQMYRE FSQQQSQDEI 

       370        380        390        400        410        420 
ARALTDLNKG HDAEDVLKQF AHRLTQKMMH PTSILLREAA QHESPDYFEW MKEQLTDVFE 

       430 
HQRKPKNNLD R

« Hide

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References

[1]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR543861 Genomic DNA. Translation: CAG69622.1.
RefSeqYP_047444.1.

3D structure databases

SMRQ6F8J3. Positions 2-400.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6F8J3.

Genome annotation databases

GeneID2878313.
GenomeReviewsGene locus ACIAD2900 in contig CR543861_GR.
KEGGaci:ACIAD2900.
NMPDRfig|62977.3.peg.2637.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHBG732626.
OMAGPILNRL.
PhylomeDBQ6F8J3.

Enzyme and pathway databases

BioCycASP62977:ACIAD2900-MONOMER.

Family and domain databases

HAMAPMF_00087. Glu-tRNA_reductase.
[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_ACIAD
AccessionPrimary (citable) accession number: Q6F8J3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: July 19, 2004
Last modified: February 9, 2010
This is version 45 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents