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Q1LIF4 (HEM1_RALME) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 69. 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:Rmet_3200
OrganismRalstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839) [Complete proteome] [HAMAP]
Taxonomic identifier266264 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length434 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.

Sequence caution

The sequence ABF10072.1 differs from that shown. Reason: Erroneous initiation.

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 – 434434Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000335063

Regions

Nucleotide binding195 – 2006NADP By similarity
Region52 – 554Substrate binding By similarity
Region120 – 1223Substrate binding By similarity

Sites

Active site531Nucleophile By similarity
Binding site1151Substrate By similarity
Binding site1261Substrate By similarity
Site1051Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1LIF4 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: BA0C9499A38CCE3D

FASTA43447,578
        10         20         30         40         50         60 
MQLLAIGINH TTAPVSLRER VAFPLEQIKP ALGALRTHLS GRNGTEAAIL STCNRTEIYC 

        70         80         90        100        110        120 
ATDVLKPGEE GFEHTLRWLA QHHNVPASEL APHLYALPQS EAVRHAFRVA SGLDSMVLGE 

       130        140        150        160        170        180 
TQILGQLKDA VRTAGEAGAL GTYLNQLFQR TFAVAKEVRG QTEIGAHSVS MAAAAVRLAQ 

       190        200        210        220        230        240 
RIFESVSTQR VLFIGAGEMI ELCATHFAAQ TPRQIVVANR TVERGEKLAE QLSEQGLTTQ 

       250        260        270        280        290        300 
AIRLQDLGDR LHEFDIVVSC TASSLPIIGL GAVERAVKRR KHRPIMMVDL AVPRDVEPEV 

       310        320        330        340        350        360 
ARLDDVFLYT VDDLGAVVRE GNALRQAAVA QAEAIIDSRV LNFMHWLETR SVVPVIRELQ 

       370        380        390        400        410        420 
SQGEAIRQAE VERARRMLAR GDDPAAVLEA LSGALTRKFL HGPTHALNHT QGEDREALLR 

       430 
LVPGLFRHSS HSER 

« Hide

References

[1]"Complete sequence of the chromosome of Ralstonia metallidurans CH34."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Martinez M., Goltsman E., Pitluck S., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Mergeay M., Benotmane M.A., Vallaeys T., Michaux A., Monchy S., Dunn J., McCorkle S., Taghavi S., van der Lelie D., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CH34 / ATCC 43123 / DSM 2839.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000352 Genomic DNA. Translation: ABF10072.1. Different initiation.
RefSeqYP_585341.1. NC_007973.1.

3D structure databases

ProteinModelPortalQ1LIF4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266264.Rmet_3200.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABF10072; ABF10072; Rmet_3200.
GeneID4040034.
KEGGrme:Rmet_3200.
PATRIC20291047. VBIRalMet4734_3593.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109650.
KOK02492.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycCMET266264:GJ5G-3421-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_RALME
AccessionPrimary (citable) accession number: Q1LIF4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: June 11, 2014
This is version 69 of the entry and version 2 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