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A9B543 (HEM1_HERA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 55. 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:Haur_3544
OrganismHerpetosiphon aurantiacus (strain ATCC 23779 / DSM 785) [Complete proteome] [HAMAP]
Taxonomic identifier316274 [NCBI]
Taxonomic lineageBacteriaChloroflexiHerpetosiphonalesHerpetosiphonaceaeHerpetosiphon

Protein attributes

Sequence length414 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 – 414414Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000093146

Regions

Nucleotide binding185 – 1906NADP By similarity
Region47 – 504Substrate binding By similarity
Region111 – 1133Substrate binding By similarity

Sites

Active site481Nucleophile By similarity
Binding site1061Substrate By similarity
Binding site1171Substrate By similarity
Site961Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A9B543 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: F5117B3104B853BD

FASTA41445,982
        10         20         30         40         50         60 
MQLVVVGAHQ RTAPISIRER IAFAEAELAQ ALSSLRQIAV EGFILSTCNR VELYALVEEA 

        70         80         90        100        110        120 
DGGRSLRQFL AQQRSIDLDE LMPHVYTYLD EDAVRHLFRV ASGLDSMALG EAQILSQIKT 

       130        140        150        160        170        180 
AYNAAQQTEL LGTTMHRLIQ AALTTGKLVR TETQLAHAQL SVVSVGLSLA RQHLDLTNRS 

       190        200        210        220        230        240 
VVIIGAGRTG ELALKHYLEY TSNITVLSRT FERAARLAEH HKVAAKPISE LAAVLQASDV 

       250        260        270        280        290        300 
VISCTSSPEL MLDFEQAQLL QAQRQRQWVL LDLAVPRDID RHVGALPEVW LYDVDDMQAI 

       310        320        330        340        350        360 
CERNRASKAA EVAGAEAIVE RELIKWQEWW LTQAVLPTIR ALRAHAEAIR LAELERTLAR 

       370        380        390        400        410 
LDLSEQQQQA VSALTSAIIN KLLHQPMRAI KDTAASPQLA HAAQQLFRLD FEAI 

« Hide

References

[1]"Complete sequence of chromosome of Herpetosiphon aurantiacus ATCC 23779."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Kim E., Bryant D.A., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 23779 / DSM 785.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000875 Genomic DNA. Translation: ABX06180.1.
RefSeqYP_001546308.1. NC_009972.1.

3D structure databases

ProteinModelPortalA9B543.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316274.Haur_3544.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX06180; ABX06180; Haur_3544.
GeneID5735403.
KEGGhau:Haur_3544.
PATRIC22124249. VBIHerAur93466_3644.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109649.
KOK02492.
OMALNKQFET.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycHAUR316274:GHYA-3581-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_HERA2
AccessionPrimary (citable) accession number: A9B543
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: January 15, 2008
Last modified: May 14, 2014
This is version 55 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