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Q1GYE9 (HEM1_METFK) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 68. 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:Mfla_2473
OrganismMethylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875) [Complete proteome] [HAMAP]
Taxonomic identifier265072 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaMethylophilalesMethylophilaceaeMethylobacillus

Protein attributes

Sequence length414 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 – 414414Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000004638

Regions

Nucleotide binding184 – 1896NADP By similarity
Region48 – 514Substrate binding By similarity
Region109 – 1113Substrate binding By similarity

Sites

Active site491Nucleophile By similarity
Binding site1041Substrate By similarity
Binding site1151Substrate By similarity
Site941Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1GYE9 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: 0C8AF430F0F13B0C

FASTA41445,810
        10         20         30         40         50         60 
MHLFTVGVNH TTAPVSIREN VAFQNEHLSG ALRDLNSHGI REAAILSTCN RTELYCNTDD 

        70         80         90        100        110        120 
PQKALEWLAN YHRLKPQAIA PYMYTLPQEN AVKHAFRVAS GLDSMVLGEA QILGQMKQAV 

       130        140        150        160        170        180 
RIAENAGTLG TLLHKLFQRT FSVAKEVRTN TNIGANSVSL AAASTRLAQR IFGALNNQHV 

       190        200        210        220        230        240 
LFIGAGEMIE LCAEHFAAHR PLSLTVANRT LERGQELAAS IGGTSMLLAD LPDRLAEFDI 

       250        260        270        280        290        300 
VITSTASQLP IVGLGMVERA IRARKHKPMF MVDLAVPRDI EPEAGELDDV FLYTVDDLAQ 

       310        320        330        340        350        360 
IVQEGMENRQ EAAAEAEAII DMRVENFMQW LKTRSAVPTI RALREQAERH RLNELEKARK 

       370        380        390        400        410 
LLARGHDPAQ VLDALSNALT NKLLHGPSHA LNSATGEDRE QLEATLRQLY QIHH 

« Hide

References

[1]"Complete sequence of Methylobacillus flagellatus KT."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J. expand/collapse author list , Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KT / ATCC 51484 / DSM 6875.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000284 Genomic DNA. Translation: ABE50738.1.
RefSeqYP_546579.1. NC_007947.1.

3D structure databases

ProteinModelPortalQ1GYE9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING265072.Mfla_2473.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABE50738; ABE50738; Mfla_2473.
GeneID4001569.
KEGGmfa:Mfla_2473.
PATRIC32270769. VBIMetFla97085_2593.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109650.
KOK02492.
OMARTEIYCA.
OrthoDBEOG6MWNBM.
ProtClustDBCLSK2529815.

Enzyme and pathway databases

BioCycMFLA265072:GHWJ-2532-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_METFK
AccessionPrimary (citable) accession number: Q1GYE9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 27, 2006
Last modified: February 19, 2014
This is version 68 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