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P42808 (HEM1_XANCH) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 89. 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
OrganismXanthomonas campestris pv. phaseoli
Taxonomic identifier29445 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaXanthomonadalesXanthomonadaceaeXanthomonas

Protein attributes

Sequence length426 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) Probable. Ref.1

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
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 – 426426Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114090

Regions

Nucleotide binding181 – 1866NADP By similarity
Region49 – 524Substrate binding By similarity
Region106 – 1083Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site1011Substrate By similarity
Binding site1121Substrate By similarity
Site911Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P42808 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 031B2DC24DE3AA2D

FASTA42646,769
        10         20         30         40         50         60 
MTLWVLGLNH QTAPVDLRER AAFAGDALPR ALESLRALPQ VSEAALLSTC NRTELYAMAE 

        70         80         90        100        110        120 
EAHSLVTWLE THAPALSGYL YQHQEAEAVR HLFRVATGLD SMVLGEPQIL GQVKDAWAVA 

       130        140        150        160        170        180 
RAHGTLGSGL DRLFQQTFSV AKRARTDTRV GANPVSVAST AVRLAQDSFA RLNESTVLLI 

       190        200        210        220        230        240 
GAGETIELAA KHLSEGRVRR LLIANRTLAH AQTLASQHGG FALPLTDLER HLAEADVVFS 

       250        260        270        280        290        300 
ATAAREPLVT RAQVEQALRA RKRKPMLLFD LAVPRDIEAS VGELSDAYLY TVDDLERAVE 

       310        320        330        340        350        360 
DNRRGRREAA DQAEAIIDLQ VARYVETLQA NARQAPLKRL RAFGDSTRDE LLAKARQQLH 

       370        380        390        400        410        420 
NGKPADEVLE QLAHALTNRL LHPPTAALRD AALNNDLELT TAADRLFPEK PGLPTSPHSY 


PDREDR 

« Hide

References

[1]"Cloning and characterization of the hemA gene for synthesis of delta-aminolevulinic acid in Xanthomonas campestris pv. phaseoli."
Asahara N., Murakami K., Korbrisate S., Hashimoto Y., Murooka Y.
Appl. Microbiol. Biotechnol. 40:846-850(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: HUT 8925.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D15073 Genomic DNA. Translation: BAA03668.1.

3D structure databases

ProteinModelPortalP42808.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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_XANCH
AccessionPrimary (citable) accession number: P42808
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: February 19, 2014
This is version 89 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