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A5N5Y0 (HEM1_CLOK5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 59. 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:CKL_0657
OrganismClostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680) [Complete proteome] [HAMAP]
Taxonomic identifier431943 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length399 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 EDK32711.1 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 – 399399Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000335022

Regions

Nucleotide binding177 – 1826NADP By similarity
Region45 – 484Substrate binding By similarity
Region106 – 1083Substrate binding By similarity

Sites

Active site461Nucleophile By similarity
Binding site1011Substrate By similarity
Binding site1121Substrate By similarity
Site911Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A5N5Y0 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: 5D94C09FD7EBFC71

FASTA39946,435
        10         20         30         40         50         60 
MIQLIGIKSQ CDIGIRQKFS ITSEVLEGKL KYINELVGSV LILSTCNRTE IYVDSNLEEK 

        70         80         90        100        110        120 
KLIDTVFYGL DWDYDLVSYI FYIKDKYAIK HLMEVSCGFH SKILGEDQIL GQIKTAYDAA 

       130        140        150        160        170        180 
LEAKTIKGKL QRLFQKAITC GKEFKHICES YRIPVSIPSI VAKEILNMDI RKYMIIGFGK 

       190        200        210        220        230        240 
IGQLLFKYLN NSQAQIIYIA VRDLNKVHDS YKKCGKIRFI SFKDRKSYYN DIDCIVSCTS 

       250        260        270        280        290        300 
APDKIISKGD LPCRKLTIFD LAVPEDIDRN VLDLDNVTLY DIDNISVIDE KNKAIRKKTM 

       310        320        330        340        350        360 
GKYRYILENH IDKFIKWEKL HQLSPEIQKV KKYGDEICEK RITTFKNKKH TKDNDILVKT 

       370        380        390 
MIESTARFYI NRAIEVMKEE KLNGREEECL RLINKIFCK 

« Hide

References

[1]"The genome of Clostridium kluyveri, a strict anaerobe with unique metabolic features."
Seedorf H., Fricke W.F., Veith B., Brueggemann H., Liesegang H., Strittmatter A., Miethke M., Buckel W., Hinderberger J., Li F., Hagemeier C., Thauer R.K., Gottschalk G.
Proc. Natl. Acad. Sci. U.S.A. 105:2128-2133(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8527 / DSM 555 / NCIMB 10680.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000673 Genomic DNA. Translation: EDK32711.1. Different initiation.
RefSeqYP_001394059.1. NC_009706.1.

3D structure databases

ProteinModelPortalA5N5Y0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING431943.CKL_0657.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEDK32711; EDK32711; CKL_0657.
GeneID5390734.
KEGGckl:CKL_0657.
PATRIC19462741. VBICloKlu111549_0717.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000090159.
KOK02492.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycCKLU431943:GJF1-657-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.
SUPFAMSSF69742. SSF69742. 1 hit.
TIGRFAMsTIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_CLOK5
AccessionPrimary (citable) accession number: A5N5Y0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: May 14, 2014
This is version 59 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