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Q3ING1 (HEM1_NATPD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 75. 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:NP_4502A
OrganismNatronomonas pharaonis (strain ATCC 35678 / DSM 2160) (Halobacterium pharaonis) [Complete proteome] [HAMAP]
Taxonomic identifier348780 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeNatronomonas

Protein attributes

Sequence length453 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 – 453453Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000004654

Regions

Nucleotide binding184 – 1896NADP By similarity
Region52 – 554Substrate binding By similarity
Region110 – 1123Substrate binding By similarity

Sites

Active site531Nucleophile By similarity
Binding site1051Substrate By similarity
Binding site1161Substrate By similarity
Site951Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3ING1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 839ADF48145910A7

FASTA45347,809
        10         20         30         40         50         60 
MTVETGIVVG ASVSHSHASI DQIETAADGS QQTAVEELLS KEGVSEAFVL QTCNRAEAYV 

        70         80         90        100        110        120 
VANDSETGTA ALAGYLAGVD DDAIRMLSHN QSLKHLMAVA CGLESLVIGE DQILGQVRDA 

       130        140        150        160        170        180 
YEDARGVGGV GPTLNDAVLK ALHVGERART ETAINEGAVS LGSAAVRFAA ERHGVTGSTA 

       190        200        210        220        230        240 
LVVGAGEMAT LAAKALDDPA SRVIVANRTR ERAERLAEEL STTASVVGVD SVDEAADAAD 

       250        260        270        280        290        300 
VVVSATGSED YVIDTADLGG VGETCVLDIA QPRDVAPGAD GIDGVAVYDL DTIESVTDEA 

       310        320        330        340        350        360 
RAKRREAAET VETMIDEEFE HLMTQYKRKR ADQVIAAMYE GAERIKAREL RTAVSKFEAE 

       370        380        390        400        410        420 
REDGLSEREH EIVESMADAL VGQLLSAPTQ SLRDAAEEDD WATINAALQL FGPGLEPEPT 

       430        440        450 
ELPTVPDGPE GVPEELRERM SSGMLEQFST NDD 

« Hide

References

[1]"Living with two extremes: conclusions from the genome sequence of Natronomonas pharaonis."
Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J., Oesterhelt D.
Genome Res. 15:1336-1343(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35678 / DSM 2160.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR936257 Genomic DNA. Translation: CAI50342.1.
RefSeqYP_330979.1. NC_007426.1.

3D structure databases

ProteinModelPortalQ3ING1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING348780.NP4502A.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAI50342; CAI50342; NP_4502A.
GeneID3702804.
KEGGnph:NP4502A.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMAHEVTGEY.

Enzyme and pathway databases

BioCycNPHA348780:GJX0-2285-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_NATPD
AccessionPrimary (citable) accession number: Q3ING1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 8, 2005
Last modified: May 14, 2014
This is version 75 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