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

B8HBS2 (HEM1_ARTCA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 43. 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:Achl_2495
OrganismArthrobacter chlorophenolicus (strain A6 / ATCC 700700 / DSM 12829 / JCM 12360) [Complete proteome] [HAMAP]
Taxonomic identifier452863 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeArthrobacter

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_1000118465

Regions

Nucleotide binding192 – 1976NADP By similarity
Region47 – 504Substrate binding By similarity
Region115 – 1173Substrate binding By similarity

Sites

Active site481Nucleophile By similarity
Binding site1101Substrate By similarity
Binding site1211Substrate By similarity
Site1001Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
B8HBS2 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: D7D32001BF5E225D

FASTA44145,570
        10         20         30         40         50         60 
MVLFSLVATH ADIDLETVAQ LSNGSSGIAA SVLSGSPAVS GAVVLATCNR YEIYGEAPNT 

        70         80         90        100        110        120 
DDVEAARAAL VAQISAQSGL AEPLVSRSFS TRTGPEVTRH LFAVSAGLDS AVVGEREIAG 

       130        140        150        160        170        180 
QVRRALITAQ HEGTASSGLV RLFQAASKTA KDVGAQTALG SRGLSIVSVA LDLATDLSEN 

       190        200        210        220        230        240 
PDWSAKKVVV FGTGAYAGAT MALLRERGCT DVSVFSSSGR AEGFVATRGG TALDADSLRP 

       250        260        270        280        290        300 
AVAAADVMIG CSGSDTRVEA DELAQVRAGS AQPLIAIDLA LTHDFDPAVG ELNGVELLTL 

       310        320        330        340        350        360 
ESVRLAAPQE QAESLAQASG IVKGAAKAFE QEREARSVDS AIVALRRHTM DVLDAEMEKV 

       370        380        390        400        410        420 
RARHGCTAAA EEVEFALRRM VKQLLHVPTV RARELAANGQ QDDYVAALEA LYGITVEQPG 

       430        440 
TAAPAAGQAE CPVDHKGLES A 

« Hide

References

[1]"Complete sequence of chromosome of Arthrobacter chlorophenolicus A6."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A6 / ATCC 700700 / DSM 12829 / JCM 12360.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001341 Genomic DNA. Translation: ACL40460.1.
RefSeqYP_002488549.1. NC_011886.1.

3D structure databases

ProteinModelPortalB8HBS2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING452863.Achl_2495.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL40460; ACL40460; Achl_2495.
GeneID7293970.
KEGGach:Achl_2495.
PATRIC20991627. VBIArtChl38304_3182.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109649.
KOK02492.
OMAPYLYVHY.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycACHL452863:GH1A-2547-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_ARTCA
AccessionPrimary (citable) accession number: B8HBS2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: May 14, 2014
This is version 43 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