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A0Q2B3 (HEM1_CLONN) 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:NT01CX_0264
OrganismClostridium novyi (strain NT) [Complete proteome] [HAMAP]
Taxonomic identifier386415 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length411 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 – 411411Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000057573

Regions

Nucleotide binding186 – 1916NADP By similarity
Region48 – 514Substrate binding By similarity
Region111 – 1133Substrate binding By similarity

Sites

Active site491Nucleophile By similarity
Binding site1061Substrate By similarity
Binding site1171Substrate By similarity
Site961Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A0Q2B3 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 73DD962E0BF8AB48

FASTA41147,552
        10         20         30         40         50         60 
MNLAVIGINY NNTPIDIREK VSFSKSQKYK ACTYLIKKGI SEIIIVSTCN RSEIYICSDE 

        70         80         90        100        110        120 
IDSHINEVVN FYKIFFNVES VNEYIFIKKD KEAVSHIYNV SAGLDSMILG EDQILGQVKE 

       130        140        150        160        170        180 
ALRYSMENKF SRKVLNKLFR EAITSAKKIK SELKISETPI SMVYIAIKLL EKNIGTLKGK 

       190        200        210        220        230        240 
KACIIGAGDM GRLALKHLIN EELEEIFVAN RTYNNVIDLL KEFPKIKLID YEKKYEILDN 

       250        260        270        280        290        300 
VDILITATAA PHLIIKKEQL QNIKQELYIM DLALPRDVEK SAGDIENIHL YDVDDFKNIS 

       310        320        330        340        350        360 
DSNKIKREEL SLIAKDSIDS YVNEFNQWMK SLKVDNTIKD LNNRCRDIKD EYLGYITKKI 

       370        380        390        400        410 
DLNERDKEIL EKMLFGALKK VVKEPILNLK ELKDEDEINK YIKSVNELFK F 

« Hide

References

[1]"The genome and transcriptomes of the anti-tumor agent Clostridium novyi-NT."
Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X., Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B., Zhou S.
Nat. Biotechnol. 24:1573-1580(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NT.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000382 Genomic DNA. Translation: ABK60902.1.
RefSeqYP_878765.1. NC_008593.1.

3D structure databases

ProteinModelPortalA0Q2B3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING386415.NT01CX_0264.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK60902; ABK60902; NT01CX_0264.
GeneID4541260.
KEGGcno:NT01CX_0264.
PATRIC19481076. VBICloNov112828_1800.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMARTEIYCA.
OrthoDBEOG6MWNBM.
ProtClustDBCLSK850017.

Enzyme and pathway databases

BioCycCNOV386415:GH98-1830-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_CLONN
AccessionPrimary (citable) accession number: A0Q2B3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 9, 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