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A6LSY3 (HEM1_CLOB8) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:Cbei_1283
OrganismClostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium acetobutylicum) [Complete proteome] [HAMAP]
Taxonomic identifier290402 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

Protein attributes

Sequence length401 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 – 401401Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000075404

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
A6LSY3 [UniParc].

Last modified July 24, 2007. Version 1.
Checksum: 813E3FA143D8A58A

FASTA40146,919
        10         20         30         40         50         60 
MIGLIGIRKN TPLEIREKFI VKSKKYNEYF GELLKELNEV VILATCNRTE IYFNASLNEE 

        70         80         90        100        110        120 
ELLKKIFDIF NWDYEYKKYV FITNNKDAYR HLFEVCSGFH SKILGEDQIL GQVKDAYEEA 

       130        140        150        160        170        180 
LEFKAVSLEL HRLFQEAITC GKRFRKEAKL FEIPVSSSSI VVSEAIKREC TKFMVLGYGE 

       190        200        210        220        230        240 
VGQLVMKYLL SHKIQTVYLV VRNPKIKDEI QDERVKVITF EEKNKYINSI ECIISCTSAP 

       250        260        270        280        290        300 
HPVVKTEDIS ESGSRLVIYD LSVPRDVEKE VALLSRTEVY NIDTISRIDD ENKKLRKDKM 

       310        320        330        340        350        360 
EDNRHIMNKY LKEYDEWLKL RSISHVIKNL KTVGNDVYEK RVQTFSHKSK DKNDIALAHK 

       370        380        390        400 
LIKSTSDFYI NRAIEVIKEE TLKGCGEEWI GIIEKIFMTK E 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000721 Genomic DNA. Translation: ABR33463.1.
RefSeqYP_001308419.1. NC_009617.1.

3D structure databases

ProteinModelPortalA6LSY3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING290402.Cbei_1283.

Proteomic databases

PRIDEA6LSY3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR33463; ABR33463; Cbei_1283.
GeneID5292507.
KEGGcbe:Cbei_1283.
PATRIC19346542. VBICloBei69853_1317.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycCBEI290402:GHL5-1355-MONOMER.
UniPathwayUPA00251; UER00316.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00087. Glu_tRNA_reductase.
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR018214. Pyrrol_synth_GluRdtase_CS.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamPF05201. 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_CLOB8
AccessionPrimary (citable) accession number: A6LSY3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: July 24, 2007
Last modified: February 19, 2014
This is version 59 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