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Q976H4 (HEM1_SULTO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 94. 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:STK_02120
OrganismSulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7) [Complete proteome] [HAMAP]
Taxonomic identifier273063 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length412 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 – 412412Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114111

Regions

Nucleotide binding189 – 1946NADP By similarity
Region52 – 554Substrate binding By similarity
Region113 – 1153Substrate binding By similarity

Sites

Active site531Nucleophile By similarity
Binding site1081Substrate By similarity
Binding site1191Substrate By similarity
Site981Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q976H4 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 37786BF228F36300

FASTA41247,333
        10         20         30         40         50         60 
MSDEFIDINN YIAIVYTYKT VGISKLYEHY VKDQELLLLK GLIKGEISVL QTCNRAETYL 

        70         80         90        100        110        120 
YTYNKEEFKD FLQKLDEIHG KQISKDAMIL KGEDAVKHLF EVASGLDSLA IGEYEILRQL 

       130        140        150        160        170        180 
KESIEKSKKL GLSSEKLEFL FKNAIKVGRK IRQQTEISKG KTGIYALAVE YAKHVSNNNI 

       190        200        210        220        230        240 
GNVKIAIVGA GEIGNKLALM LKNEGAQNVT IFNRTYEKAL EVANKYGFKA EPLDFYKINN 

       250        260        270        280        290        300 
YDIVFVAIYY DKKINLPNPK LVIDLSVPQI VLGNNVITLE NLRSISDKIM ETKILSLQKA 

       310        320        330        340        350        360 
EELIHIEIEN FKNEIIKYNQ NRLISKFMKR IEDIREAEIN RAYAEILKHA NDKEEIKNII 

       370        380        390        400        410 
DKMTNSMLKK IFSPLFETVR KNEDMANYIN NIFEILSNGN ISNSKTEEAK EK 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000023 Genomic DNA. Translation: BAB65173.1.
RefSeqNP_376064.1. NC_003106.2.

3D structure databases

ProteinModelPortalQ976H4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273063.ST0212.

Proteomic databases

PRIDEQ976H4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB65173; BAB65173; STK_02120.
GeneID1458103.
KEGGsto:ST0212.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000107850.
KOK02492.
OMAKGMAVHF.
ProtClustDBPRK00045.

Enzyme and pathway databases

BioCycSTOK273063:GJC7-238-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.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_SULTO
AccessionPrimary (citable) accession number: Q976H4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: December 1, 2001
Last modified: February 19, 2014
This is version 94 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