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Q60172 (HEM1_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:MJ0143
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length392 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
Reference 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 – 392392Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114101

Regions

Nucleotide binding165 – 1706NADP By similarity
Region38 – 414Substrate binding By similarity
Region91 – 933Substrate binding By similarity

Sites

Active site391Nucleophile By similarity
Binding site861Substrate By similarity
Binding site971Substrate By similarity
Site761Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q60172 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: 952E1CFDCDA3874C

FASTA39244,847
        10         20         30         40         50         60 
MIILKADYKK YNVSELEKLR MDEEKFYETF DNAILLQTCN RVEIIFDADS LEEIKGIENI 

        70         80         90        100        110        120 
DLEKFDILFG DKAIEHLFRV ACGLESMIVG EDQILGQLKN AYLKAKEKGR ISKKLEKIIL 

       130        140        150        160        170        180 
KAIHTGQRAR VETKINEGGV SIGSAAVELA EKIFGLEGKN VLLIGAGEMA NLVIKALKEK 

       190        200        210        220        230        240 
NIKAIIVANR TYEKAEKLAK ELGGMAIKFD KLEEALRYAD IVISATGAPH PILNKERLKN 

       250        260        270        280        290        300 
AGKTIIIDIA NPRDTTDDIR ELPDIFLFTI DDLRLVAEEN LKKRKEEIPK VEMIICEELE 

       310        320        330        340        350        360 
RLKEFLDKMR FETAIKELGQ YIENVRKKEV EKAKKILKNK NKPVEEVLED FSKALCKRII 

       370        380        390 
YDIIKIFENV EDKEVFECLA KEFKKLGNKN KN 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77117 Genomic DNA. Translation: AAB98126.1.
PIRH64317.
RefSeqNP_247111.1. NC_000909.1.

3D structure databases

ProteinModelPortalQ60172.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243232.MJ0143.

Proteomic databases

PRIDEQ60172.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB98126; AAB98126; MJ_0143.
GeneID1450987.
KEGGmja:MJ_0143.

Phylogenomic databases

eggNOGCOG0373.
KOK02492.
OMAMANLVIK.
ProtClustDBPRK00045.

Enzyme and pathway databases

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_METJA
AccessionPrimary (citable) accession number: Q60172
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: February 19, 2014
This is version 101 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

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names