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A6LKW9 (HEM1_THEM4) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 58. 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:Tmel_0706
OrganismThermosipho melanesiensis (strain BI429 / DSM 12029) [Complete proteome] [HAMAP]
Taxonomic identifier391009 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermosipho

Protein attributes

Sequence length368 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 – 368368Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000004716

Regions

Nucleotide binding164 – 1696NADP By similarity
Region43 – 464Substrate binding By similarity
Region94 – 963Substrate binding By similarity

Sites

Active site441Nucleophile By similarity
Binding site891Substrate By similarity
Binding site1001Substrate By similarity
Site791Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A6LKW9 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 6074AC5A541663BC

FASTA36842,784
        10         20         30         40         50         60 
MKLNLVGLGR NTPIYILEKF DFDEQEFFSS LKVKTTEVAV LKTCHRREIY YIGDKEPLTI 

        70         80         90        100        110        120 
NEIIEPYIIR KSGIDVVRHL FKVSCGLDSM VLGEHQILSQ VKNTHKNFCH GKILNKLFNE 

       130        140        150        160        170        180 
AVSLGKEART KTGINKYPLS ISYIAVKLIE EQINIEGKKI FVIGTGMMGQ KVIKYLVSRG 

       190        200        210        220        230        240 
ADIYISNRTI KKAYEIKKMF SEVNIVDFEE KYKHISSSDV VISATNAPHY VVEEKKVNSQ 

       250        260        270        280        290        300 
KNIIFIDLSM PRNIEPSIKE YHTLYTLEDL NEISKKYNKL RQEKISTIQN LIETRIKKFL 

       310        320        330        340        350        360 
TWYKLQTVKD DILYIQNLAE KLVYEEIEKL SKKILLDDNS LKQIQKSLKS CTKKIVSYHI 


NYIKEKVI 

« Hide

References

[1]"Complete sequence of Thermosipho melanesiensis BI429."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N. expand/collapse author list , Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BI429 / DSM 12029.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000716 Genomic DNA. Translation: ABR30570.1.
RefSeqYP_001305955.1. NC_009616.1.

3D structure databases

ProteinModelPortalA6LKW9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING391009.Tmel_0706.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR30570; ABR30570; Tmel_0706.
GeneID5297066.
KEGGtme:Tmel_0706.
PATRIC23922617. VBITheMel19269_0736.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMAVANGVHR.
OrthoDBEOG6MWNBM.
ProtClustDBCLSK975882.

Enzyme and pathway databases

BioCycTMEL391009:GHM1-752-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_THEM4
AccessionPrimary (citable) accession number: A6LKW9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 24, 2007
Last modified: February 19, 2014
This is version 58 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