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A1W4B9 (HEM1_ACISJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamyl-tRNA reductase

Short name=GluTR
EC=1.2.1.70
Gene names
Name:hemA
Ordered Locus Names:Ajs_0852
OrganismAcidovorax sp. (strain JS42) [Complete proteome] [HAMAP]
Taxonomic identifier232721 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length436 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

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

Pathway

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

Subunit structure

Homodimer By similarity. HAMAP-Rule 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-Rule 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.

Sequence similarities

Belongs to the glutamyl-tRNA reductase family.

Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processprotoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionNADP binding

Inferred from electronic annotation. Source: InterPro

glutamyl-tRNA reductase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 436436Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000335002

Regions

Nucleotide binding194 – 1996NADP By similarity
Region56 – 594Substrate binding By similarity
Region119 – 1213Substrate binding By similarity

Sites

Active site571Nucleophile By similarity
Binding site1141Substrate By similarity
Binding site1251Substrate By similarity
Site1041Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A1W4B9 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 961B91D9ACA90712

FASTA43647,070
        10         20         30         40         50         60 
MAVWALGINH HTAPLDLRGR FAFALDQIAP TLHGLRDSLS SASGRHPGVE TAIISTCNRT 

        70         80         90        100        110        120 
EIYCAAEAPA LDHTLDWLAH SGGVSPALLR SHSYSLENGL VARHAFRVAS GLDSMVLGEA 

       130        140        150        160        170        180 
QILGQMKDAV RAAEGAGALG TTLNQLFQRS FAVAKEVRTS TDIGAHSISM AAAAVRLAGQ 

       190        200        210        220        230        240 
LFEDLSQIRV LFVGAGEMIE LCTTHFAAKN PKQISIANRT LERGEKLAAR FGGDVMRLAD 

       250        260        270        280        290        300 
LPDHLHEYDA VISCTASSLP IIGLGAVERS LKKRRHRPMF MVDLAVPRDI EPEVQQLQDA 

       310        320        330        340        350        360 
YLYTVDDLAS VVQTAQAHRQ AAVAQAEAII DAGVQSFVHW MELRSPATQN GGVVPLIQQL 

       370        380        390        400        410        420 
NSQADEWRAL EIARAKKRLA KGEDIETVLE ALSRGLTQKM LHGTMAELRA GDAEARAQTA 

       430 
QAVSRLFLRS HSKNGL 

« Hide

References

[1]"Complete sequence of chromosome 1 of Acidovorax sp. JS42."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JS42.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000539 Genomic DNA. Translation: ABM41094.1.
RefSeqYP_985170.1. NC_008782.1.

3D structure databases

ProteinModelPortalA1W4B9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING232721.Ajs_0852.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM41094; ABM41094; Ajs_0852.
GeneID4674150.
KEGGajs:Ajs_0852.
PATRIC20686972. VBIAciSp27161_1041.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109650.
KOK02492.
OMAKMLHGTM.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycASP232721:GHWE-856-MONOMER.
UniPathwayUPA00251; UER00316.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00087. Glu_tRNA_reductase.
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_dimer.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR018214. Pyrrol_synth_GluRdtase_CS.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
SUPFAMSSF69075. SSF69075. 1 hit.
SSF69742. SSF69742. 1 hit.
TIGRFAMsTIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_ACISJ
AccessionPrimary (citable) accession number: A1W4B9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 6, 2007
Last modified: May 14, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways