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A2SD47 (HEM1_METPP) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:Mpe_A0524
OrganismMethylibium petroleiphilum (strain PM1) [Complete proteome] [HAMAP]
Taxonomic identifier420662 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesMethylibium

Protein attributes

Sequence length443 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

Porphyrin-containing compound metabolism; chlorophyll biosynthesis. 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 processChlorophyll biosynthesis
Porphyrin biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processchlorophyll biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

protoporphyrinogen 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 – 443443Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000004641

Regions

Nucleotide binding193 – 1986NADP By similarity
Region55 – 584Substrate binding By similarity
Region118 – 1203Substrate binding By similarity

Sites

Active site561Nucleophile By similarity
Binding site1131Substrate By similarity
Binding site1241Substrate By similarity
Site1031Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A2SD47 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 5C7CD8BC95659C2F

FASTA44347,837
        10         20         30         40         50         60 
MSVFALGLNH TTAPVDLRGR FAFTLEQLAP TLQGFRERLT TGQRPGTPEA AILSTCNRTE 

        70         80         90        100        110        120 
LYCAAEPQLV RPALEWLAGV GGVGADTLSH HAYMLEGGEA ARHAFRVASG LDSMVLGEPQ 

       130        140        150        160        170        180 
ILGQMKQAVR EADAAGTLGS TLHQLFQRSF AVAKEVRTAT EIGTHSISMA AAAVRLAAQL 

       190        200        210        220        230        240 
FEDLREIRVL FVGAGEMIEL AATHFSARAP ARMAVANRTL ERGERLASRF GAESIRLSDL 

       250        260        270        280        290        300 
PQRLHEFDAV VSCTASSLPL IGLGAVERAL KVRRHRPIFM VDLAVPRDIE PEVARLDDVY 

       310        320        330        340        350        360 
LYTVDDLSAI VQSGGEKRLA AVAQAEAIIE TGVQSFVHWL GQRGTVPLIQ ALNAQADSWR 

       370        380        390        400        410        420 
ENELVRARKL LARGESVDAV LDALSRGLTQ KMLHGTLAEL HASDPAQRAQ LATTVSRLFL 

       430        440 
RGAIPPDAVR PSGPREDDHL DGV 

« Hide

References

[1]"Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1."
Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R.
J. Bacteriol. 189:1931-1945(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PM1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000555 Genomic DNA. Translation: ABM93486.1.
RefSeqYP_001019721.1. NC_008825.1.

3D structure databases

ProteinModelPortalA2SD47.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING420662.Mpe_A0524.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABM93486; ABM93486; Mpe_A0524.
GeneID4787347.
KEGGmpt:Mpe_A0524.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109650.
KOK02492.
OMARTEIYCA.
OrthoDBEOG6MWNBM.
ProtClustDBPRK00045.

Enzyme and pathway databases

BioCycMPET420662:GHBE-531-MONOMER.
UniPathwayUPA00251; UER00316.
UPA00668.

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_METPP
AccessionPrimary (citable) accession number: A2SD47
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: March 6, 2007
Last modified: February 19, 2014
This is version 61 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