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C5C5B0 (HEM1_BEUC1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 40. 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:Bcav_4009
OrganismBeutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432) [Complete proteome] [HAMAP]
Taxonomic identifier471853 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeBeutenbergiaceaeBeutenbergia

Protein attributes

Sequence length441 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 – 441441Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000202630

Regions

Nucleotide binding204 – 2096NADP By similarity
Region48 – 514Substrate binding By similarity
Region129 – 1313Substrate binding By similarity

Sites

Active site491Nucleophile By similarity
Binding site1241Substrate By similarity
Binding site1351Substrate By similarity
Site1141Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
C5C5B0 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: 0AF8243E92066449

FASTA44145,703
        10         20         30         40         50         60 
MLLSVSASHR DADLADLERL SSGVGRVWAD APLVAHGLDG AGVVLLATCN RFEVYLDVAD 

        70         80         90        100        110        120 
GTDPQRALAV VRDLVRTVPE SPLAAPGADD DAAGPGPDPS AALRVRVGDD AARHLFGVAS 

       130        140        150        160        170        180 
GLDSIVVGER EIAGQVRRAI AAARRAGTTT GALERLFAQA QRTSRAVEAG TGLAAAGRSV 

       190        200        210        220        230        240 
VGVALDLAAR SAPPWPLARV VLIGTGSYAG ASLAALRARG CTDVRVHSES GRAEEFARAR 

       250        260        270        280        290        300 
EAEAVPPGEL LTAIADADVV VSCRGSVRPV LDAAAVAGAR AAAERRAEER AGHAVGTAVQ 

       310        320        330        340        350        360 
PRPLVVVDLA LHRDVDPAVG SVDGVELLDL GTIRAHAPAA ATRDVERARE IVDDAVAQHA 

       370        380        390        400        410        420 
LVRAAREMDP AITRLRGRVR EVLDAEVGRL PVGPVSREDA ERALHRLAAT LAHAPTEAAR 

       430        440 
EAARAGRGEE YVEALRLLFP D 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001618 Genomic DNA. Translation: ACQ82250.1.
RefSeqYP_002884012.1. NC_012669.1.

3D structure databases

ProteinModelPortalC5C5B0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING471853.Bcav_4009.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACQ82250; ACQ82250; Bcav_4009.
GeneID7861107.
KEGGbcv:Bcav_4009.
PATRIC21098740. VBIBeuCav91323_4061.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109649.
KOK02492.
OMAEHAPAEH.
OrthoDBEOG6MWNBM.
ProtClustDBCLSK2812319.

Enzyme and pathway databases

BioCycBCAV471853:GI1Z-4062-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. 2 hits.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_BEUC1
AccessionPrimary (citable) accession number: C5C5B0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: February 19, 2014
This is version 40 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