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Q93ST4 (HEM1_CHLTE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 100. 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:CT1426
OrganismChlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS) [Reference proteome] [HAMAP]
Taxonomic identifier194439 [NCBI]
Taxonomic lineageBacteriaChlorobiChlorobiaChlorobialesChlorobiaceaeChlorobaculum

Protein attributes

Sequence length426 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

Porphyrin-containing compound metabolism; chlorophyll biosynthesis. 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.

Sequence caution

The sequence AAG12432.1 differs from that shown. Reason: Frameshift at position 319.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 426426Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_0000114007

Regions

Nucleotide binding189 – 1946NADP By similarity
Region49 – 524Substrate binding By similarity
Region114 – 1163Substrate binding By similarity

Sites

Active site501Nucleophile By similarity
Binding site1091Substrate By similarity
Binding site1201Substrate By similarity
Site991Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q93ST4 [UniParc].

Last modified August 30, 2002. Version 2.
Checksum: A7122C2C947D2429

FASTA42648,133
        10         20         30         40         50         60 
MNIISVGVNH KTAPIEIRER IALSEVQNKE LVTDLVSSGL ASEAMVVSTC NRTELYVVPG 

        70         80         90        100        110        120 
MPEVNCDYLK DYIISYKNAR NAVRPEHFFS RFYCGTARHL FEVSCAIDSL VLGEGQILGQ 

       130        140        150        160        170        180 
VKNAYRIAAE VGTAGILLTR LCHTAFSVAK KVKTRTKLME GAVSVSYAAV ELAQKIFSNL 

       190        200        210        220        230        240 
SMKKVLLIGA GETGELAAKH MYAKNARNIV ITNRTQSKAE ALAEELGTNR VLPYESYKEH 

       250        260        270        280        290        300 
LHEFDIIITA VSTKEYILNA AEMQQSMAKR RLKPVIILDL GLPRNVDPEV GALQNMFLKD 

       310        320        330        340        350        360 
IDALKHIIDK NLERRRAELP KVKAIIDEEL VAFGQWLNTL KVRPTIVDLQ SKFLEIKEKE 

       370        380        390        400        410        420 
LERYRYKVSE EELRRMEHLT DRILKKILHH PIKMLKAPVD TADNIPSKVN LVRNIFDLEE 


PNQSLQ 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY005138 Genomic DNA. Translation: AAG12432.1. Frameshift.
AE006470 Genomic DNA. Translation: AAM72654.1.
RefSeqNP_662312.1. NC_002932.3.

3D structure databases

ProteinModelPortalQ93ST4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING194439.CT1426.

Protocols and materials databases

DNASU1006241.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM72654; AAM72654; CT1426.
GeneID1006241.
KEGGcte:CT1426.
PATRIC21400779. VBIChlTep116050_1294.

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMALAHKLTN.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycCTEP194439:GHN0-1465-MONOMER.
UniPathwayUPA00251; UER00316.
UPA00668.

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_CHLTE
AccessionPrimary (citable) accession number: Q93ST4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 3, 2002
Last sequence update: August 30, 2002
Last modified: May 14, 2014
This is version 100 of the entry and version 2 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