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A9WPH1 (HEM1_RENSM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 51. 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:RSal33209_1218
OrganismRenibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235) [Complete proteome] [HAMAP]
Taxonomic identifier288705 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeRenibacterium

Protein attributes

Sequence length440 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 – 440440Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000335064

Regions

Nucleotide binding181 – 1866NADP By similarity
Region40 – 434Substrate binding By similarity
Region105 – 1073Substrate binding By similarity

Sites

Active site411Nucleophile By similarity
Binding site1001Substrate By similarity
Binding site1111Substrate By similarity
Site901Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A9WPH1 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: D97066F78C188072

FASTA44045,781
        10         20         30         40         50         60 
MNVVVLFSLV ATHADIDLET VARLSAGSAA VSTSTVVLAT CNRFEIYSAA ENPATARAEM 

        70         80         90        100        110        120 
EAALAHATGF APSLVSSSFK LLTGTDVAKH LFAVASGLDS AVVGEREIAG QVRRALIDAQ 

       130        140        150        160        170        180 
TAFPVPGPLV RLFQTASRTA KDVGSQTALG SQGRSIVSVA LDLAGDSSAT AWDQRKAVVF 

       190        200        210        220        230        240 
GTGAYAGVTM ALLRERGVSD LSVYSSSGRA ADFVASRGGT AAESLEEALG SADLVIGCSG 

       250        260        270        280        290        300 
SDQRVSAETL ADIRRRTGTA GEPLSVIDLA LSRDFDPAIT ELPGVELLTL ETVRLAAPSE 

       310        320        330        340        350        360 
QESALLQTQV IVSRAAADFE LSIATRSVDT AIVALRKHTM AVLDAEMERV RAQHGCTAAA 

       370        380        390        400        410        420 
EEVEFALRRM VKQLLHGPTV RARELAAAGQ QAEYIAALQS LYGIELESPT PAAQPVESIP 

       430        440 
AVEPASCPVN HNAVDRSQSA 

« Hide

References

[1]"Genome sequence of the fish pathogen Renibacterium salmoninarum suggests reductive evolution away from an environmental Arthrobacter ancestor."
Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S., Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H., Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.
J. Bacteriol. 190:6970-6982(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000910 Genomic DNA. Translation: ABY22956.1.
RefSeqYP_001624370.1. NC_010168.1.

3D structure databases

ProteinModelPortalA9WPH1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING288705.RSal33209_1218.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY22956; ABY22956; RSal33209_1218.
GeneID5822473.
KEGGrsa:RSal33209_1218.
PATRIC23075677. VBIRenSal21953_1259.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109649.
KOK02492.
OMAIGCSGSD.
ProtClustDBPRK00045.

Enzyme and pathway databases

BioCycRSAL288705:GHX1-1218-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.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_RENSM
AccessionPrimary (citable) accession number: A9WPH1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: February 19, 2014
This is version 51 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