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Reviewed, UniProtKB/Swiss-Prot Q1ITN7 (HEM11_ACIBL)

Last modified November 3, 2009. Version 32. 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 1
      Short name=GluTR 1
    EC=1.2.1.70
Gene names
Name: hemA1
Ordered Locus Names: Acid345_0758
OrganismAcidobacteria bacterium (strain Ellin345) [Complete proteome] [HAMAP]
Taxonomic identifier204669 [NCBI]
Taxonomic lineageBacteria › Acidobacteria › Candidatus Koribacter

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Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

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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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 1 HAMAP MF_00087
PRO_0000334998

Regions

Nucleotide binding190 – 1956NADP By similarity
Region51 – 544Substrate binding By similarity
Region115 – 1173Substrate binding By similarity

Sites

Active site521Nucleophile By similarity
Binding site1101Substrate By similarity
Binding site1211Substrate By similarity
Site1001Important for activity By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q1ITN7-1 [UniParc].

Last modified June 13, 2006. Version 1.
Checksum: 289915A299EE391E

FASTA43147,868
        10         20         30         40         50         60 
MEPSLVVVGL NFKTSPVAVR ERFWMSELRR YEALHQLVRA EGIDELVVLA TCNRTEFILW 

        70         80         90        100        110        120 
TSDAGEAADS VLRFLTHEYG LKMSDWSHFY RLMDDVALNH IFRVASSLDS MVIGEPEIVG 

       130        140        150        160        170        180 
QFKNAWSQAQ AAGTTGRFLD AVMQKALTVS KRVRNETAIG NAAVSIPYTT VELSKQVLGE 

       190        200        210        220        230        240 
LFDKAVVLMG AGKMSESAAK YLMNHGASQI CVINRTLHKA QEFSEKVGGI AVALEDRAPY 

       250        260        270        280        290        300 
LDHADIIVSS TSCPHYVIEK ADAERIQAAR GGKPIVMVDI AVPRDIDPAV REVPGVHLFD 

       310        320        330        340        350        360 
MDDLEKVAKR NESERQVAAV AAEEILADEA KGFRRKLMAE RVVPTIVALR NRLDEVCRQE 

       370        380        390        400        410        420 
LESLRQELGP FTEDQDQAMT ALTAHITQRI AGSLARELKE LPERSEQDML TMAVQRLFHL 

       430 
EQPQKAAAGT N

« Hide

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Cross-references

Sequence databases

CP000360 Genomic DNA. Translation: ABF39763.1.
RefSeqYP_589837.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ1ITN7.

Genome annotation databases

GeneID4068634.
GenomeReviewsGene locus Acid345_0758 in contig CP000360_GR.
KEGGaba:Acid345_0758.
NMPDRfig|204669.6.peg.750.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1ITN7.
OMARIELYAD.

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 nameHEM11_ACIBL
AccessionPrimary (citable) accession number: Q1ITN7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 13, 2006
Last modified: November 3, 2009
This is version 32 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