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A9WIS2 (HEM1_CHLAA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:Caur_2593
OrganismChloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl) [Reference proteome] [HAMAP]
Taxonomic identifier324602 [NCBI]
Taxonomic lineageBacteriaChloroflexiChloroflexalesChloroflexaceaeChloroflexus

Protein attributes

Sequence length434 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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 434434Glutamyl-tRNA reductase HAMAP-Rule MF_00087
PRO_1000075402

Regions

Nucleotide binding193 – 1986NADP By similarity
Region54 – 574Substrate binding By similarity
Region118 – 1203Substrate binding By similarity

Sites

Active site551Nucleophile By similarity
Binding site1131Substrate By similarity
Binding site1241Substrate By similarity
Site1031Important for activity By similarity

Sequences

Sequence LengthMass (Da)Tools
A9WIS2 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 1A101A099F052555

FASTA43447,312
        10         20         30         40         50         60 
MNLFLAGLDH TTAPVEIREQ LAFSQTDLPS ALMQLTSSET GTPPLFAEAV ILSTCNRVEL 

        70         80         90        100        110        120 
YGVTNPGTTA QHVVDFLAAF HRRPAASFVH TLYFYQGEAV ARHLCATAAG LRSLVLGEAQ 

       130        140        150        160        170        180 
IQGQVRNAYE AAQRIGSVGS ILHRLFQIAL VAGKRVRHET TIGKGAASVS QAGVELARRR 

       190        200        210        220        230        240 
LGDLRGREVL LIGGGEVSEL AAQNLIANGA DRLTIVNRTS ARAAALAERY GAEMLDFGAL 

       250        260        270        280        290        300 
PQALARADIV ISSTAAPVPI IYRHHVAEAI AHKQRARACG ECDPPTMLLI DLAVPRDIAA 

       310        320        330        340        350        360 
DVAQIPGVHL FTVDDLREVV SHTIELRSAV LEIAQQIVEE QVQEFLSWMR TQEALPVLTM 

       370        380        390        400        410        420 
LRQRAEEVRN EELARALRRL HDLSPEQRAV IEGLSRSIVN KLLHLPTRCL REAAAHGQGK 

       430 
RYASILAELF NLEH 

« Hide

References

[1]"Complete genome sequence of the filamentous anoxygenic phototrophic bacterium Chloroflexus aurantiacus."
Tang K.H., Barry K., Chertkov O., Dalin E., Han C.S., Hauser L.J., Honchak B.M., Karbach L.E., Land M.L., Lapidus A., Larimer F.W., Mikhailova N., Pitluck S., Pierson B.K., Blankenship R.E.
BMC Genomics 12:334-334(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29366 / DSM 635 / J-10-fl.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000909 Genomic DNA. Translation: ABY35799.1.
RefSeqYP_001636188.1. NC_010175.1.

3D structure databases

ProteinModelPortalA9WIS2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING324602.Caur_2593.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABY35799; ABY35799; Caur_2593.
GeneID5827062.
KEGGcau:Caur_2593.
PATRIC21416349. VBIChlAur28763_2921.

Phylogenomic databases

eggNOGCOG0373.
HOGENOMHOG000109650.
KOK02492.
OMALAHKLTN.
OrthoDBEOG6MWNBM.

Enzyme and pathway databases

BioCycCAUR324602:GIXU-2637-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.
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.
ProtoNetSearch...

Entry information

Entry nameHEM1_CHLAA
AccessionPrimary (citable) accession number: A9WIS2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: May 14, 2014
This is version 52 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