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C3PKG1 (HEM1_CORA7) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 39. 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:cauri_0298
OrganismCorynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CN-1) (Corynebacterium nigricans) [Complete proteome] [HAMAP]
Taxonomic identifier548476 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length458 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 – 458458Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000190514

Regions

Nucleotide binding191 – 1966NADP By similarity
Region49 – 524Substrate binding By similarity
Region114 – 1163Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site1091Substrate By similarity
Binding site1201Substrate By similarity
Site991Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
C3PKG1 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 925C261543213257

FASTA45849,388
        10         20         30         40         50         60 
MSVLVVGMSH QSAPVALLEK LSMDETVQND TCRAMVSAGS LSEAMIISTC NRLEVYTVTN 

        70         80         90        100        110        120 
SFHSGVQDVV HNLAEVSGVE EEKLRSYLYV RYADAAAEHL MMVTSGLDSM VVGEQQIIGQ 

       130        140        150        160        170        180 
VRTAYQFASE QGTVGPRIHA LAQSALRTGK RVHSETEIDE AGSSMVSFAF DQALSRMGRE 

       190        200        210        220        230        240 
DLAGKRVLIL GAGAMASLAA THAGRLGAHL IIANRTIARA ERVAQHAHEA GVYADVIDFS 

       250        260        270        280        290        300 
ERAQALRDVD VAISATGAQG FTITAADVER YHVADRELML VDLSLPRDID DAVAEAEGVD 

       310        320        330        340        350        360 
LINIERLNNS LQAADTDLAA GTSPHAQARR IVSEELESYA SEQRVRDVVP AVSALRKRAA 

       370        380        390        400        410        420 
NLVQCEVARM EQKHPELDER QMGDINRALK RVADKLLHEP TVRAKQLAAN SGTVSHETAL 

       430        440        450 
QELFGLQLEG SGVAVDMAEL PDAAQMEAAE NTKEEKDA 

« Hide

References

[1]"Complete genome sequence and lifestyle of black-pigmented Corynebacterium aurimucosum ATCC 700975 (formerly C. nigricans CN-1) isolated from a vaginal swab of a woman with spontaneous abortion."
Trost E., Gotker S., Schneider J., Schneiker-Bekel S., Szczepanowski R., Tilker A., Viehoever P., Arnold W., Bekel T., Blom J., Gartemann K.H., Linke B., Goesmann A., Puhler A., Shukla S.K., Tauch A.
BMC Genomics 11:91-91(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700975 / DSM 44827 / CN-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001601 Genomic DNA. Translation: ACP31897.1.
RefSeqYP_002833835.1. NC_012590.1.

3D structure databases

ProteinModelPortalC3PKG1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING169292.cauri_0298.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACP31897; ACP31897; cauri_0298.
GeneID7801153.
KEGGcar:cauri_0298.
PATRIC21476536. VBICorAur68407_0319.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109649.
KOK02492.
OMAPYLYVHY.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycCAUR548476:GH9E-309-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_CORA7
AccessionPrimary (citable) accession number: C3PKG1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 16, 2009
Last modified: May 14, 2014
This is version 39 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