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A5D3L4 (HEM1_PELTS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. 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:PTH_0971
OrganismPelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI) [Complete proteome] [HAMAP]
Taxonomic identifier370438 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaePelotomaculum

Protein attributes

Sequence length444 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 – 444444Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000075416

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
A5D3L4 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: CE7874AB66E30749

FASTA44449,167
        10         20         30         40         50         60 
MLILVVGLNH RTAPVEVREK LSFSAKSLQG ALAQLKSYPV IEGCAILSTC NRTEIYAATL 

        70         80         90        100        110        120 
EMDDGLNAIW DFLSRWSGVG ISEIKNFTYS HTLYDTIRHL FRVAAGLDSM ILGETQILGQ 

       130        140        150        160        170        180 
VREAYQRAIE YESTNRVLNT LFQQAITVGK RVRTETGIDR NAVSISYAAV ELARQHLGSL 

       190        200        210        220        230        240 
DGRSVLVIGA GKMSELTARH LVANGVSSVI VSNRSFERAV ALAEQFRGRA VRFDELYRCM 

       250        260        270        280        290        300 
EAADIVISCT AASHCVVKAE EVSRVMDKRR GRAIFMVDIA VPRDIEAEVG NLAGVTLFDI 

       310        320        330        340        350        360 
DDLKNVIDQN LAERKQAAVK AEEIIEEELD GFMKWLGMQF VVPTISALKK WGDEIKQKEL 

       370        380        390        400        410        420 
CRALNRLGNI SEHDRKVICS MANSIVNQIL HVPVAQLKSY ALTTEGHLYT EILQNLFNLD 

       430        440 
VPGQKPKKQP APAGIKEPVL AKKG 

« Hide

References

[1]"The genome of Pelotomaculum thermopropionicum reveals niche-associated evolution in anaerobic microbiota."
Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.
Genome Res. 18:442-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13744 / JCM 10971 / SI.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009389 Genomic DNA. Translation: BAF59152.1.
RefSeqYP_001211521.1. NC_009454.1.

3D structure databases

ProteinModelPortalA5D3L4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING370438.PTH_0971.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF59152; BAF59152; PTH_0971.
GeneID5140131.
KEGGpth:PTH_0971.
PATRIC22908973. VBIPelThe8413_1091.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMARTEIYCA.
OrthoDBEOG6MWNBM.
ProtClustDBPRK00045.

Enzyme and pathway databases

BioCycPTHE370438:GCGQ-1007-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.
TIGRFAMsTIGR01035. hemA. 1 hit.
PROSITEPS00747. GLUTR. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHEM1_PELTS
AccessionPrimary (citable) accession number: A5D3L4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: June 12, 2007
Last modified: February 19, 2014
This is version 56 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