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A4X1U1 (HEM1_SALTO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:Strop_0356
OrganismSalinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440) [Complete proteome] [HAMAP]
Taxonomic identifier369723 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicromonosporineaeMicromonosporaceaeSalinispora

Protein attributes

Sequence length455 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 – 455455Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000075424

Regions

Nucleotide binding190 – 1956NADP By similarity
Region49 – 524Substrate binding By similarity
Region114 – 1163Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site1091Substrate By similarity
Binding site1201Substrate By similarity
Site991Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A4X1U1 [UniParc].

Last modified May 29, 2007. Version 1.
Checksum: E11D84256B38311B

FASTA45547,268
        10         20         30         40         50         60 
MKLLVVGASY RTAPVAALER LTVAPADLSR VLTRLVAQPY VSEAVLVSTC NRVEVYAVVS 

        70         80         90        100        110        120 
GFHGGLGDIC AVLAESTGCQ PAALADHLYV HFDAAAVNHV FRVAVGLDSM VVGEAQILGQ 

       130        140        150        160        170        180 
LRDAYHWASE AETVGRLLHE LMQQALRVGK RAHSETGIDR AGQSVVTAAL GLATELLHSD 

       190        200        210        220        230        240 
LACRPALVVG AGAMGSLGVA TLARLGAGPV SVTNRGVDRA IRLAESYGAT AVPIADLTAT 

       250        260        270        280        290        300 
LSTVDIVVAA TAAPEAVLTR AVVTQALAGR NPSRGPLVLL DLAVPRDVEP GVADLPGVQV 

       310        320        330        340        350        360 
IDIDRMAALV ADGPVAADAA AVEQIVAAEV DTFLTWLRGA DVAPTVAALR GRADDVVAAE 

       370        380        390        400        410        420 
LGRLVHRRPD LTDEQRADVA RTVHRVVQRL LHQPTVRVRQ LAAEPGGDQY TALLRELFDL 

       430        440        450 
EVPQTSAVGT VPDVVVPDVD PQLGGDAEAP PTGGE 

« Hide

References

[1]"Complete sequence of Salinispora tropica CNB-440."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Sun H., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Jensen P.R., Moore B.S., Udwary D.W., Richardson P.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-916 / DSM 44818 / CNB-440.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000667 Genomic DNA. Translation: ABP52841.1.
RefSeqYP_001157219.1. NC_009380.1.

3D structure databases

ProteinModelPortalA4X1U1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING369723.Strop_0356.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABP52841; ABP52841; Strop_0356.
GeneID5056794.
KEGGstp:Strop_0356.
PATRIC23439601. VBISalTro43511_0367.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109649.
KOK02492.
OMARTEIYCA.
OrthoDBEOG6MWNBM.
ProtClustDBPRK00045.

Enzyme and pathway databases

BioCycSTRO369723:GI49-365-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.
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.
ProtoNetSearch...

Entry information

Entry nameHEM1_SALTO
AccessionPrimary (citable) accession number: A4X1U1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 29, 2007
Last modified: February 19, 2014
This is version 60 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