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B9KGB2 (HEM1_CAMLR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 44. 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:Cla_0770
OrganismCampylobacter lari (strain RM2100 / D67 / ATCC BAA-1060) [Complete proteome] [HAMAP]
Taxonomic identifier306263 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length435 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 – 435435Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000190510

Regions

Nucleotide binding189 – 1946NADP By similarity
Region50 – 534Substrate binding By similarity
Region115 – 1173Substrate binding By similarity

Sites

Active site511Nucleophile By similarity
Binding site1101Substrate By similarity
Binding site1211Substrate By similarity
Site1001Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
B9KGB2 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 041D663FB91B6B3B

FASTA43549,314
        10         20         30         40         50         60 
MHYYCISFTH KNTDIATREK LSFSNEDKKR ELLKLIHTNN KILESLVLST CNRVEIFLFV 

        70         80         90        100        110        120 
GDVESINEHI LKTLSLLCGV DRENLSTKAD FYEDSGAIHH LFSVASSLDS LVIGETQIAG 

       130        140        150        160        170        180 
QLKDAYKFAL QEQRCGVHLT RAVHYAFKCA ANVRNQTEIS KNPISVASVA VAKAKELVNL 

       190        200        210        220        230        240 
ENKTAVVVGA GEMSELACKH LLNAKAKVLI LNRDIQNAQK LCEDLGENAS YESIANLKEA 

       250        260        270        280        290        300 
LNQYEIFFSA TNAPHAIITN DLLEEKDYSR YFFDIAVPRD IDVKANEKNI VYAVDDLEEV 

       310        320        330        340        350        360 
VRKNLTLREH QAQIAYSIVG TMTNEFFQHL SKLATLPLVK QLRLQADEIA KEQLQKAIDK 

       370        380        390        400        410        420 
GYLKHSNHEE ARKLIRQVMN AFLHHPSVNL KKLSGTMQND SVINAMRYVF DLKNENMEGL 

       430 
NLYKCEFNLE NNHEI 

« Hide

References

[1]"The complete genome sequence and analysis of the human pathogen Campylobacter lari."
Miller W.G., Wang G., Binnewies T.T., Parker C.T.
Foodborne Pathog. Dis. 5:371-386(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM2100 / D67 / ATCC BAA-1060.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000932 Genomic DNA. Translation: ACM64097.1.
RefSeqYP_002575348.1. NC_012039.1.

3D structure databases

ProteinModelPortalB9KGB2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING306263.Cla_0770.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM64097; ACM64097; Cla_0770.
GeneID7410104.
KEGGcla:Cla_0770.
PATRIC20062007. VBICamLar15090_0749.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109651.
KOK02492.
OMAKMLHGTM.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycCLAR306263:GH7X-769-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_CAMLR
AccessionPrimary (citable) accession number: B9KGB2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 14, 2014
This is version 44 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