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Reviewed, UniProtKB/Swiss-Prot O28304 (HEM1_ARCFU)

Last modified June 16, 2009. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Glutamyl-tRNA reductase
      Short name=GluTR
    EC=1.2.1.70
Gene names
Name: hemA
Ordered Locus Names: AF_1975
OrganismArchaeoglobus fulgidus [Complete proteome] [HAMAP]
Taxonomic identifier2234 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus

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Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA) By similarity.

Catalytic activity

L-glutamate 1-semialdehyde + NADP+ + tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. HAMAP MF_00087

Pathway

Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. HAMAP MF_00087

Subunit structure

Homodimer By similarity.

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.

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.

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Ontologies

Keywords
   Biological processPorphyrin biosynthesis
   LigandNADP
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processoxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

porphyrin biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: InterPro

   Molecular functionNADP or NADPH binding

Inferred from electronic annotation. Source: InterPro

glutamyl-tRNA reductase activity

Inferred from electronic annotation. Source: HAMAP

shikimate 5-dehydrogenase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 437437Glutamyl-tRNA reductase HAMAP MF_00087
PRO_0000114098

Regions

Nucleotide binding177 – 1826NADP By similarity
Region46 – 494Substrate binding By similarity
Region102 – 1043Substrate binding By similarity

Sites

Active site471Nucleophile By similarity
Binding site971Substrate By similarity
Binding site1081Substrate By similarity
Site871Important for activity By similarity

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Sequences

Sequence LengthMass (Da)Tools
O28304-1 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: DD0A999D55790CD6

FASTA43748,442
        10         20         30         40         50         60 
MEIGCITISH KNAKVEEIEK IWLTVKPRLE DVISKCSFSE YAYIFTCNRF EIYLVGENLK 

        70         80         90        100        110        120 
SCLQDIAEEL GITGKAEIFV GESCLRHLLR VASGIESMIV GEEQILGQVR QCFNLCREGG 

       130        140        150        160        170        180 
QAGEVLERVF GKAVQVGRRV RRETAISKGS VSIGSAAVEV AERVLGTLKG KKALLVGAGE 

       190        200        210        220        230        240 
MGTLVAKAIA GKEVEAVLIA NRTYEKAEEL AKRIGGVAVK FDKLVDYLKV CDVVISATSA 

       250        260        270        280        290        300 
PHAVITRGDV ERAMRERSQK LLIIDIALPR DVDESVAQLD GVELLTIDDL RRISEENLAR 

       310        320        330        340        350        360 
RREEIAKVEG IIEEELEQLK LLLKDISARD AIAAMYSLAE RFVGEEVEEL YAKLNARYGV 

       370        380        390        400        410        420 
SEDVKEILND FANSLIKKFL REPTVRLREA ARKDEFHVIE SIKYVFGDGN GRVSEGKDAK 

       430 
VEEGKPEVDV QRSKAES

« Hide

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Cross-references

Sequence databases

AE000782 Genomic DNA. Translation: AAB89281.1.
PIRF69496.
RefSeqNP_070799.1.

3D structure databases

HSSPHSSP built from PDB template 1GPJ based on UniProtKB Q9UXR8.
ModBaseSearch...

Genome annotation databases

GeneID1485197.
GenomeReviewsGene locus AF_1975 in contig AE000782_GR.
KEGGafu:AF1975.
NMPDRfig|224325.1.peg.1960.
TIGRAF_1975.

Phylogenomic databases

HOGENOMO28304.
OMAO28304. IDIAQPR.

Enzyme and pathway databases

BioCycAFUL224325:AF_1975-MON.
BRENDA1.2.1.70. 7576.

Family and domain databases

HAMAPMF_00087.
[Tree]
InterProIPR000343. 4pyrrol_synth_GluRdtase.
IPR015896. 4pyrrol_synth_GluRdtase_C.
IPR015895. 4pyrrol_synth_GluRdtase_N.
IPR016040. NAD(P)-bd_dom.
IPR018214. pyrrol_synth_GluRdtase_CS.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PfamPF00745. GlutR_dimer. 1 hit.
PF05201. GlutR_N. 1 hit.
PF01488. Shikimate_DH. 1 hit.
[Graphical view]
PIRSFPIRSF000445. 4pyrrol_synth_GluRdtase. 1 hit.
TIGRFAMsTIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameHEM1_ARCFU
AccessionPrimary (citable) accession number: O28304
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: June 16, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents