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C3KDC5 (HEM1_PSEFS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 41. 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:PFLU_0737
OrganismPseudomonas fluorescens (strain SBW25) [Complete proteome] [HAMAP]
Taxonomic identifier216595 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length429 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 – 429429Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000202640

Regions

Nucleotide binding187 – 1926NADP By similarity
Region49 – 524Substrate binding By similarity
Region112 – 1143Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site1071Substrate By similarity
Binding site1181Substrate By similarity
Site971Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
C3KDC5 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 959466EDB03B03C4

FASTA42946,669
        10         20         30         40         50         60 
MAFLALGINH KTASVDVRER VAFTPEQLVE ALQQLCRLTD SREAAILSTC NRSELYIEQE 

        70         80         90        100        110        120 
HLSADVVLRW LADYHHLDLD DLRASAYVHE DDAAVRHMMR VASGLDSLVL GEPQILGQMK 

       130        140        150        160        170        180 
SAYAVAREAG TVGPLLGRLF QATFNSAKQV RTDTAIGENP VSVAFAAVSL AKQIFSDLQR 

       190        200        210        220        230        240 
SQALLIGAGE TITLVARHLH DLGVKRIVVA NRTLERASIL AEQFGAHAVL LADIPAELVR 

       250        260        270        280        290        300 
SDIVISSTAS QLPILGKGAV ESALKLRKHK PIFMVDIAVP RDIEPEVGEL DDVYLYSVDD 

       310        320        330        340        350        360 
LHEVVAENLK SRQGAAQAAE EMVSAGADDF MVRLRELAAV DVLKAYRQQG ERLRDEELLK 

       370        380        390        400        410        420 
AQRLLANGSS AEDVLVQLAR GLTNKLLHAP SVQLKKLTAE GRLDALAMAQ ELFALGEGAS 


DSSSDKKLQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM181176 Genomic DNA. Translation: CAY47005.1.
RefSeqYP_002870401.1. NC_012660.1.

3D structure databases

ProteinModelPortalC3KDC5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING216595.PFLU0737.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAY47005; CAY47005; PFLU_0737.
GeneID7818005.
KEGGpfs:PFLU0737.
PATRIC19895696. VBIPseFlu98510_0971.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
KOK02492.
OMARTEIYCA.
OrthoDBEOG6MWNBM.
ProtClustDBPRK00045.

Enzyme and pathway databases

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_PSEFS
AccessionPrimary (citable) accession number: C3KDC5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: June 16, 2009
Last modified: February 19, 2014
This is version 41 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