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A6Q3S5 (HEM1_NITSB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 53. 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:NIS_1024
OrganismNitratiruptor sp. (strain SB155-2) [Complete proteome] [HAMAP]
Taxonomic identifier387092 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaNitratiruptor

Protein attributes

Sequence length432 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 – 432432Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000057577

Regions

Nucleotide binding190 – 1956NADP By similarity
Region50 – 534Substrate binding By similarity
Region115 – 1173Substrate binding By similarity

Sites

Active site511Nucleophile By similarity
Binding site1101Substrate By similarity
Binding site1211Substrate By similarity
Site1001Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A6Q3S5 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: E0F4DCE8BFEA4EE5

FASTA43249,015
        10         20         30         40         50         60 
MQYLVVSFSH KNTDIVTREK LALSDDNKRE DVATTLLQNP VINEAIILST CNRIEIILSV 

        70         80         90        100        110        120 
KDPFSATEAV LKKLSEVSGI NYEELEGRAD IYEDNGAIHH VFSVASGLDS LVVGETQITG 

       130        140        150        160        170        180 
QIKDAYKEAY EKGWCGQKLG RVMHYAFKCS KEVRSSTDIT RSPVSVASAA VSMAKEKLGN 

       190        200        210        220        230        240 
LGGMSALVVG AGEMGRLAAK HLISHGCNVI LVGRDLEKTK TVAQEIDPDI RVEHVSNLQK 

       250        260        270        280        290        300 
LINSYRLLFS ATSSKNPVIT KDMVKEQSFD RYWFDMAVPR DIEEIYVARI HYFAVDDLKE 

       310        320        330        340        350        360 
IVNKNMAFRE EQARNAYKIV GHHVNEFFKW LQTLEIDPII KEIRKRAKDS ALAELQKAIK 

       370        380        390        400        410        420 
KGYIPKEYEK SIEKLLHNAF NRFLHDPTKQ LKAIADEPRA DTIVEAIKFF FEIEEEVGLN 

       430 
RYKCEYYMNL RS 

« Hide

References

[1]"Deep-sea vent epsilon-proteobacterial genomes provide insights into emergence of pathogens."
Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K., Horikoshi K.
Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SB155-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009178 Genomic DNA. Translation: BAF70134.1.
RefSeqYP_001356491.1. NC_009662.1.

3D structure databases

ProteinModelPortalA6Q3S5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING387092.NIS_1024.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF70134; BAF70134; NIS_1024.
GeneID5361241.
KEGGnis:NIS_1024.
PATRIC22684128. VBINitSp82229_1068.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMALAHKLTN.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycNSP387092:GHA5-1063-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_NITSB
AccessionPrimary (citable) accession number: A6Q3S5
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 21, 2007
Last modified: May 14, 2014
This is version 53 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