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A3MXT2 (HEM12_PYRCJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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 2

Short name=GluTR 2
EC=1.2.1.70
Gene names
Name:hemA2
Ordered Locus Names:Pcal_2034
OrganismPyrobaculum calidifontis (strain JCM 11548 / VA1) [Complete proteome] [HAMAP]
Taxonomic identifier410359 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiThermoprotealesThermoproteaceaePyrobaculum

Protein attributes

Sequence length391 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 – 391391Glutamyl-tRNA reductase 2 HAMAP-Rule MF_00087
PRO_0000335099

Regions

Nucleotide binding177 – 1826NADP By similarity
Region47 – 504Substrate binding By similarity
Region103 – 1053Substrate binding By similarity

Sites

Active site481Nucleophile By similarity
Binding site981Substrate By similarity
Binding site1091Substrate By similarity
Site881Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A3MXT2 [UniParc].

Last modified April 3, 2007. Version 1.
Checksum: 6A6F2690806753F0

FASTA39142,346
        10         20         30         40         50         60 
MDFLAPLSAV VLTYREVGGD ALGALAEEMR KCAEELAKAT PMFVLHTCGR VEVYLYGASE 

        70         80         90        100        110        120 
EEVARVAARY RRFAEGVKVL RGAEAARHLF AVAAGLDSML IGETDILGQL EEAYDRQVKA 

       130        140        150        160        170        180 
GYTRGLLKTV VERAVRVGKR VRTETGISRG PRGLGSLAVM YVSRMLDLRE ASVAVLGAGA 

       190        200        210        220        230        240 
VGAGLAMELA ARGVKRLVVL NRTYEKAVEV ANRVGGEARP LTEEEVEKCL AECDVVFSSV 

       250        260        270        280        290        300 
HTLQPVIKRV PPEARVKVIV DLGVPSSVVP NLPVAVVKIE DLRELAEEYN RERAGEVEKA 

       310        320        330        340        350        360 
WAIVDEEVAR LPRLLARRYV EEATSAIMAQ AMAAAEEEGK RAGCDTAVLA AKTTVKRTLL 

       370        380        390 
PLITKLKEMA ENGKAEEAAK LIQLLQEALQ S 

« Hide

References

[1]"Complete sequence of Pyrobaculum calidifontis JCM 11548."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Cozen A.E., Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: JCM 11548 / VA1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000561 Genomic DNA. Translation: ABO09449.1.
RefSeqYP_001056915.1. NC_009073.1.

3D structure databases

ProteinModelPortalA3MXT2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING410359.Pcal_2034.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO09449; ABO09449; Pcal_2034.
GeneID4908889.
KEGGpcl:Pcal_2034.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000112880.
KOK02492.
OMAKGMAVHF.
ProtClustDBPRK00045.

Enzyme and pathway databases

BioCycPCAL410359:GIX2-2083-MONOMER.
UniPathwayUPA00251; UER00316.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_00087. Glu_tRNA_reductase.
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR018214. Pyrrol_synth_GluRdtase_CS.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamPF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
SUPFAMSSF69742. SSF69742. 1 hit.
TIGRFAMsTIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM12_PYRCJ
AccessionPrimary (citable) accession number: A3MXT2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 3, 2007
Last modified: February 19, 2014
This is version 60 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