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Q18F28 (HEM1_HALWD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 73. 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:HQ_3336A
OrganismHaloquadratum walsbyi (strain DSM 16790 / HBSQ001) [Complete proteome] [HAMAP]
Taxonomic identifier362976 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloquadratum

Protein attributes

Sequence length454 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 – 454454Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000335088

Regions

Nucleotide binding182 – 1876NADP By similarity
Region50 – 534Substrate binding By similarity
Region108 – 1103Substrate binding By similarity

Sites

Active site511Nucleophile By similarity
Binding site1031Substrate By similarity
Binding site1141Substrate By similarity
Site931Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q18F28 [UniParc].

Last modified July 25, 2006. Version 1.
Checksum: 2D20D329DCA6FDDC

FASTA45448,625
        10         20         30         40         50         60 
MNTGVICGVR VSHNRASVEE IELAGERDSR TIMETLLTRD GITESFAIQT CNRSEAYVVA 

        70         80         90        100        110        120 
DGAVAGRRAL ASFAPDVRDG AVVDMSHEES LRHLLRVATG LESLVLGEDQ ILGQFKRAIE 

       130        140        150        160        170        180 
VARGIGALGP MLEAGVTKAI HVGERARSET SINEGAVSIG SAAVRLAGQS VGLNGRKALV 

       190        200        210        220        230        240 
IGAGEMGSLV AESLASTNIS EVVIANRTIE NAESIAETIN SPAYAVSLDS LTEVITEASI 

       250        260        270        280        290        300 
IMTATGYGKY LIEPTDIDGA GETFIIDLAQ PRNVHPATAD IENAIVQDID ALESITKETE 

       310        320        330        340        350        360 
ASRQAAAREV DAMIDEEFDR LLESYKRQRA DEAISEMYEA AEHVKRREVE TALEKLEKQG 

       370        380        390        400        410        420 
TLTDNQRETI SSMADTLINQ LLAAPTKSLR DAAAEDDWTT IQTAMTLFDP NFGGDTPQPD 

       430        440        450 
RPDDIPRAAE RGDISGDDLP DDVPNHIAEK VSDG 

« Hide

References

[1]"The genome of the square archaeon Haloquadratum walsbyi: life at the limits of water activity."
Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F., Pfeiffer F., Oesterhelt D.
BMC Genomics 7:169-169(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 16790 / HBSQ001.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM180088 Genomic DNA. Translation: CAJ53433.1.
RefSeqYP_659025.1. NC_008212.1.

3D structure databases

ProteinModelPortalQ18F28.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING362976.HQ3336A.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ53433; CAJ53433; HQ_3336A.
GeneID4194102.
KEGGhwa:HQ3336A.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMAEHMIEDE.

Enzyme and pathway databases

BioCycHWAL362976:GJSR-2460-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_HALWD
AccessionPrimary (citable) accession number: Q18F28
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 25, 2006
Last modified: May 14, 2014
This is version 73 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