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Q2LQU3 (HEM1_SYNAS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. 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:SYNAS_05720
ORF Names:SYN_02274
OrganismSyntrophus aciditrophicus (strain SB) [Complete proteome] [HAMAP]
Taxonomic identifier56780 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaSyntrophobacteralesSyntrophaceaeSyntrophus

Protein attributes

Sequence length423 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 ABC76451.1 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 – 423423Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000335076

Regions

Nucleotide binding191 – 1966NADP By similarity
Region49 – 524Substrate binding By similarity
Region116 – 1183Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site1111Substrate By similarity
Binding site1221Substrate By similarity
Site1011Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2LQU3 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: FD4811CCA61A5ED5

FASTA42347,114
        10         20         30         40         50         60 
MGILLIGMSH KTSPLAVRER FSLSCENRDH PLDRIRQMPS IREALYLATC NRVEVLVSAA 

        70         80         90        100        110        120 
EEAEQAVEEG LKALMAERGG ISGQELERCL YTLSGAEAVR HLFRVASSLD SLVMGEPQIL 

       130        140        150        160        170        180 
GQVKEAYREA VEHGVTGILL NRILHHAFQV AKRVRTETGI ADNAVSVGYA AVELAKKIFG 

       190        200        210        220        230        240 
RLDGKVILLV GAGEMSELAA RHLLKQGIKS IFVANRTHAR ALEMAEQFEG KAVVLEQVPE 

       250        260        270        280        290        300 
VLKSVDIVIS STGASNYVLT RDMVAAALRR RKNRFLFLID IAVPRDIEPA AGDIDNVYLY 

       310        320        330        340        350        360 
NIDHLQELVD ENRNHRLREA EKAEAIIEEE VGNHTAWLST LDVVPTIVEF REKIEGIMKA 

       370        380        390        400        410        420 
ELGKSASWRH SLSEIDQRHV ESLMASIVNK ILHEPTACLR EQSRNRNGKA YAAALRKLFK 


LER 

« Hide

References

[1]"The genome of the syntrophic bacterium Syntrophus aciditrophicus: Life dependent on negative change in electrical potential."
Gunsalus R., Rohlin L., Kim U., Krupp R., Bhattacharyya A., Campbell J., Mclerney M., Moutakki H., Rio-Hernandez L.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SB.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000252 Genomic DNA. Translation: ABC76451.1. Different initiation.
RefSeqYP_460619.1. NC_007759.1.

3D structure databases

ProteinModelPortalQ2LQU3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING56780.SYN_02274.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC76451; ABC76451; SYN_02274.
GeneID3885135.
KEGGsat:SYN_02274.
PATRIC23861605. VBISynAci70500_0623.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycSACI56780:GHXT-583-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_SYNAS
AccessionPrimary (citable) accession number: Q2LQU3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: February 19, 2014
This is version 66 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