Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0C2E3 (HEM1_CLOPE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:CPE1437
OrganismClostridium perfringens (strain 13 / Type A) [Complete proteome] [HAMAP]
Taxonomic identifier195102 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length400 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 – 400400Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114013

Regions

Nucleotide binding179 – 1846NADP By similarity
Region45 – 484Substrate binding By similarity
Region108 – 1103Substrate binding By similarity

Sites

Active site461Nucleophile By similarity
Binding site1031Substrate By similarity
Binding site1141Substrate By similarity
Site931Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
P0C2E3 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 037AC2CFD4F60DEE

FASTA40045,890
        10         20         30         40         50         60 
MIGVIGVKRN VDIAIREKLA LYPKKHKKYV GELLNSFKEV VILNTCNRTE IYFNCTEEIS 

        70         80         90        100        110        120 
EDEIFDKIFN VFNWNDDLKK YMFLSKEKRA VTHLMEVICG FHSRILGEDQ ILGQIKDAYK 

       130        140        150        160        170        180 
TAISDNSISS ELQKMFEIAI ACGKKFKTEC KMFEVPVSSV SISINSALLK GCRKFMVLGY 

       190        200        210        220        230        240 
GEIGKLAIKH LLSHKVECIY LIVRDKSKAS DLEGEIVEVL DFNEKNQVIN EVDCIVSCTA 

       250        260        270        280        290        300 
APHTVVRNED IKTEGDIIHI YDLAVPRDVD KELSEKERVI LKDIDEISKI DDKNKKIRKE 

       310        320        330        340        350        360 
RMEEYKHIVE ESIEEFLNWL KIREVSSKIR NIKIRENEIC SERIKTFSNK GNGENAKLAE 

       370        380        390        400 
RMIKSTADAY VNRAIELLKS EALKGSDSSC AEIIEKIFLT 

« Hide

References

[1]"Complete genome sequence of Clostridium perfringens, an anaerobic flesh-eater."
Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T., Ogasawara N., Hattori M., Kuhara S., Hayashi H.
Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 13 / Type A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000016 Genomic DNA. Translation: BAB81143.1.
RefSeqNP_562353.1. NC_003366.1.

3D structure databases

ProteinModelPortalP0C2E3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195102.CPE1437.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB81143; BAB81143; BAB81143.
GeneID989747.
KEGGcpe:CPE1437.
PATRIC19496823. VBICloPer59675_1507.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000090159.
KOK02492.
OMAMANLVIK.
OrthoDBEOG6MWNBM.
ProtClustDBPRK00045.

Enzyme and pathway databases

BioCycCPER195102:GJFM-1483-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_CLOPE
AccessionPrimary (citable) accession number: P0C2E3
Secondary accession number(s): Q9ZND3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: February 19, 2014
This is version 60 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